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Structured Review

ATCC human oxa1l

A, hypothetical structural organization of <t>Oxa1L</t> in the inner membrane (IM) is shown. Oxa1L is composed of an N-terminal domain in the intermembrane space (IMS), a transmembrane domain (TMD) with five transmembrane helices, and a C-terminal domain located in the matrix. B, the primary sequence of the Oxa1L-CTT expressed and purified from E. coli is shown. Regions predicted to be α-helical by the secondary structure prediction programs on Biology Workbench using the PELE collection of programs are underlined. The methionine (M) at the beginning of the sequence and the LEHis6 at the C terminus of the sequence are from the vector. C, the Rosetta structure prediction protocol was used to generate a model of Oxa1L-CTT (26). The structure shown is the lowest free-energy structure and is displayed using PyMOL. D, prediction of coiled-coil formation is shown. The coiled-coil structure was predicted using the COILS program with two different windows. The figure shows the comparison of coiled-coil-forming tendency in a 14-residue window of the C-terminal tail of yeast, human, bovine, and mouse Oxa1. The amino acid listed as zero in the figure corresponds to residues 317, 334, 334, and 330 residues in full-length yeast, human, bovine, and mouse Oxa1, respectively.

Human Oxa1l, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes * "

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M110.148262

A, hypothetical structural organization of Oxa1L in the inner membrane (IM) is shown. Oxa1L is composed of an N-terminal domain in the intermembrane space (IMS), a transmembrane domain (TMD) with five transmembrane helices, and a C-terminal domain located in the matrix. B, the primary sequence of the Oxa1L-CTT expressed and purified from E. coli is shown. Regions predicted to be α-helical by the secondary structure prediction programs on Biology Workbench using the PELE collection of programs are underlined. The methionine (M) at the beginning of the sequence and the LEHis6 at the C terminus of the sequence are from the vector. C, the Rosetta structure prediction protocol was used to generate a model of Oxa1L-CTT (26). The structure shown is the lowest free-energy structure and is displayed using PyMOL. D, prediction of coiled-coil formation is shown. The coiled-coil structure was predicted using the COILS program with two different windows. The figure shows the comparison of coiled-coil-forming tendency in a 14-residue window of the C-terminal tail of yeast, human, bovine, and mouse Oxa1. The amino acid listed as zero in the figure corresponds to residues 317, 334, 334, and 330 residues in full-length yeast, human, bovine, and mouse Oxa1, respectively.

Figure Legend Snippet: A, hypothetical structural organization of Oxa1L in the inner membrane (IM) is shown. Oxa1L is composed of an N-terminal domain in the intermembrane space (IMS), a transmembrane domain (TMD) with five transmembrane helices, and a C-terminal domain located in the matrix. B, the primary sequence of the Oxa1L-CTT expressed and purified from E. coli is shown. Regions predicted to be α-helical by the secondary structure prediction programs on Biology Workbench using the PELE collection of programs are underlined. The methionine (M) at the beginning of the sequence and the LEHis6 at the C terminus of the sequence are from the vector. C, the Rosetta structure prediction protocol was used to generate a model of Oxa1L-CTT (26). The structure shown is the lowest free-energy structure and is displayed using PyMOL. D, prediction of coiled-coil formation is shown. The coiled-coil structure was predicted using the COILS program with two different windows. The figure shows the comparison of coiled-coil-forming tendency in a 14-residue window of the C-terminal tail of yeast, human, bovine, and mouse Oxa1. The amino acid listed as zero in the figure corresponds to residues 317, 334, 334, and 330 residues in full-length yeast, human, bovine, and mouse Oxa1, respectively.

Techniques Used: Sequencing, Purification, Plasmid Preparation

Effect of protein concentration, salt, and TFE on the secondary structure of Oxa1L-CTT determined by CD. A, shown is the effect of Oxa1L-CTT concentration (0.1, 0.2, and 0.34 mg/ml) on the CD spectra. B, shown is the effect of salt concentration on the CD spectra of Oxa1L-CTT. The protein concentration was 0.1 mg/ml. C, shown is the effect of TFE concentration on the CD spectra of Oxa1L-CTT. Protein concentration was 0.2 mg/ml.

Figure Legend Snippet: Effect of protein concentration, salt, and TFE on the secondary structure of Oxa1L-CTT determined by CD. A, shown is the effect of Oxa1L-CTT concentration (0.1, 0.2, and 0.34 mg/ml) on the CD spectra. B, shown is the effect of salt concentration on the CD spectra of Oxa1L-CTT. The protein concentration was 0.1 mg/ml. C, shown is the effect of TFE concentration on the CD spectra of Oxa1L-CTT. Protein concentration was 0.2 mg/ml.

Techniques Used: Protein Concentration, Concentration Assay

Oligomerization of Oxa1L-CTT. A, shown is the effect of KCl on oligomerization of Oxa1L-CTT as examined by analytical ultracentrifugation. The panels show the representative equilibrium sedimentation profiles at three different KCl concentrations at 10 mm MgCl2. The data are plotted as the absorption of Oxa1L-CTT (0.6 mg/ml) at 280 nm versus the distance from the center of the axis of rotation (radius). The lower section of each panel shows the raw data in closed circles. The lines represent the best fits. The upper panels show the residual for the corresponding given fit. The global fit of three protein concentrations (0.3, 0.6, and 0.9 mg/ml) is not shown. The data presented here were obtained at 24,000 rpm. B, detection of dimer and tetramer formation of Oxa1L-CTT by DMS cross-linking followed by Western blotting as described in “Experimental Procedures” is shown.

Figure Legend Snippet: Oligomerization of Oxa1L-CTT. A, shown is the effect of KCl on oligomerization of Oxa1L-CTT as examined by analytical ultracentrifugation. The panels show the representative equilibrium sedimentation profiles at three different KCl concentrations at 10 mm MgCl2. The data are plotted as the absorption of Oxa1L-CTT (0.6 mg/ml) at 280 nm versus the distance from the center of the axis of rotation (radius). The lower section of each panel shows the raw data in closed circles. The lines represent the best fits. The upper panels show the residual for the corresponding given fit. The global fit of three protein concentrations (0.3, 0.6, and 0.9 mg/ml) is not shown. The data presented here were obtained at 24,000 rpm. B, detection of dimer and tetramer formation of Oxa1L-CTT by DMS cross-linking followed by Western blotting as described in “Experimental Procedures” is shown.

Techniques Used: Sedimentation, Western Blot

Interaction of the mammalian mitochondrial large ribosomal subunit (39 S) with Oxa1L-CTT analyzed by surface plasma resonance. A, shown is the RU change of Oxa1L-CTT binding to 39 S (circles) and 28 S (triangles) as a function of Oxa1L-CTT concentrations. Ribosomes (39 S and 28 S) and BSA were immobilized on a L1 sensor chip, and Oxa1L-CTT was flowed through the cell as described under “Experimental Procedures.” The RU values were recorded for each injection after 15 s of buffer exchange. The value of the RU from the cell carrying BSA has been subtracted from each value. The solid circles represent experimental data, and the line represents a sigmoidal fit. B, the salt dependence of the RU change when Oxa1L-CTT (20 μl at 0.18 μm) was used in buffer containing different KCl concentrations and injected at a flow rate of 10 μl/min, and RU values were noted from the base line after 15 s of buffer exchange.

Figure Legend Snippet: Interaction of the mammalian mitochondrial large ribosomal subunit (39 S) with Oxa1L-CTT analyzed by surface plasma resonance. A, shown is the RU change of Oxa1L-CTT binding to 39 S (circles) and 28 S (triangles) as a function of Oxa1L-CTT concentrations. Ribosomes (39 S and 28 S) and BSA were immobilized on a L1 sensor chip, and Oxa1L-CTT was flowed through the cell as described under “Experimental Procedures.” The RU values were recorded for each injection after 15 s of buffer exchange. The value of the RU from the cell carrying BSA has been subtracted from each value. The solid circles represent experimental data, and the line represents a sigmoidal fit. B, the salt dependence of the RU change when Oxa1L-CTT (20 μl at 0.18 μm) was used in buffer containing different KCl concentrations and injected at a flow rate of 10 μl/min, and RU values were noted from the base line after 15 s of buffer exchange.

Techniques Used: Binding Assay, Injection, Buffer Exchange

Estimation of the thermodynamic parameters governing the interaction of Oxa1L-CTT with mitochondrial 55 S ribosomes using isothermal titration calorimetry. A, raw data for the binding of Oxa1L-CTT to 55 S ribosomes provided as the power output (μcal/s) as a function of time are shown. The protein concentration was 80 μm (syringe), and the 55 S ribosome concentration was 4 μm (cell). The first injection is only for the purpose of the experimental setup and is ignored for data analysis. B, shown is the amount of heat evolved at each injection normalized to the number of moles of Oxa1L-CTT injected (kcal/mol) versus the molar ratio of Oxa1L-CTT to 55 S ribosome. The solid line represents the nonlinear least squares fit for the data.

Figure Legend Snippet: Estimation of the thermodynamic parameters governing the interaction of Oxa1L-CTT with mitochondrial 55 S ribosomes using isothermal titration calorimetry. A, raw data for the binding of Oxa1L-CTT to 55 S ribosomes provided as the power output (μcal/s) as a function of time are shown. The protein concentration was 80 μm (syringe), and the 55 S ribosome concentration was 4 μm (cell). The first injection is only for the purpose of the experimental setup and is ignored for data analysis. B, shown is the amount of heat evolved at each injection normalized to the number of moles of Oxa1L-CTT injected (kcal/mol) versus the molar ratio of Oxa1L-CTT to 55 S ribosome. The solid line represents the nonlinear least squares fit for the data.

Techniques Used: Isothermal Titration Calorimetry, Binding Assay, Protein Concentration, Concentration Assay, Injection

Strategy used to identify ribosomal proteins near the Oxa1L binding site. Oxa1L-CTT was incubated with 39 S subunits and cross-linked to nearby proteins using DMS as described under “Experimental Procedures.” Cross-linked complexes were purified by centrifugation through a sucrose cushion. The ribosomes were then denatured, and ribosomal proteins cross-linked to Oxa1L-CTT were recovered on Ni-NTA. Cross-linked proteins were digested with trypsin, and the proteins present were identified by LC/MS/MS.

Figure Legend Snippet: Strategy used to identify ribosomal proteins near the Oxa1L binding site. Oxa1L-CTT was incubated with 39 S subunits and cross-linked to nearby proteins using DMS as described under “Experimental Procedures.” Cross-linked complexes were purified by centrifugation through a sucrose cushion. The ribosomes were then denatured, and ribosomal proteins cross-linked to Oxa1L-CTT were recovered on Ni-NTA. Cross-linked proteins were digested with trypsin, and the proteins present were identified by LC/MS/MS.

Techniques Used: Binding Assay, Incubation, Purification, Centrifugation, Liquid Chromatography with Mass Spectroscopy

Peptides and ion scores of ribosomal proteins cross-linked to Oxa1L-CTT Ion scores of greater than 35 are considered significant.

Figure Legend Snippet: Peptides and ion scores of ribosomal proteins cross-linked to Oxa1L-CTT Ion scores of greater than 35 are considered significant.

Techniques Used: Sequencing

A, structural representation the putative binding site of Oxa1L mapped onto the structure of the Thermus thermophilus 50 S subunit (PDB coordinate 2WRL) using PyMOL. A, shown is a representation of the exit tunnel on bacterial ribosomes showing the traditional proteins (L22, L23, L24, and L29) near to exit tunnel of the 50 S ribosomal subunit. B, shown is a representation of the mammalian mitochondrial ribosomal proteins homologous to bacterial L13, L20, and L28 (space-filled) modeled onto the bacterial 50 S subunit. The regions of the rRNA missing in the mammalian mitochondrial ribosome have been manually removed from the coordinates for the 50 S subunit. In E. coli, L28 is almost completely covered by rRNA, but these segments of rRNA are missing in the 39 S subunit, leaving L28 more exposed to solvent. C, shown is a comparison of the sizes of bacterial and yeast L13, L20, and L28 with mitochondrial homologs. L20 is absent in yeast. The molecular weights of the MRPs are estimated after the removal of import signals predicated by MitoProt II.

Figure Legend Snippet: A, structural representation the putative binding site of Oxa1L mapped onto the structure of the Thermus thermophilus 50 S subunit (PDB coordinate 2WRL) using PyMOL. A, shown is a representation of the exit tunnel on bacterial ribosomes showing the traditional proteins (L22, L23, L24, and L29) near to exit tunnel of the 50 S ribosomal subunit. B, shown is a representation of the mammalian mitochondrial ribosomal proteins homologous to bacterial L13, L20, and L28 (space-filled) modeled onto the bacterial 50 S subunit. The regions of the rRNA missing in the mammalian mitochondrial ribosome have been manually removed from the coordinates for the 50 S subunit. In E. coli, L28 is almost completely covered by rRNA, but these segments of rRNA are missing in the 39 S subunit, leaving L28 more exposed to solvent. C, shown is a comparison of the sizes of bacterial and yeast L13, L20, and L28 with mitochondrial homologs. L20 is absent in yeast. The molecular weights of the MRPs are estimated after the removal of import signals predicated by MitoProt II.

Techniques Used: Binding Assay

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Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: A, hypothetical structural organization of Oxa1L in the inner membrane (IM) is shown. Oxa1L is composed of an N-terminal domain in the intermembrane space (IMS), a transmembrane domain (TMD) with five transmembrane helices, and a C-terminal domain located in the matrix. B, the primary sequence of the Oxa1L-CTT expressed and purified from E. coli is shown. Regions predicted to be α-helical by the secondary structure prediction programs on Biology Workbench using the PELE collection of programs are underlined. The methionine (M) at the beginning of the sequence and the LEHis6 at the C terminus of the sequence are from the vector. C, the Rosetta structure prediction protocol was used to generate a model of Oxa1L-CTT (26). The structure shown is the lowest free-energy structure and is displayed using PyMOL. D, prediction of coiled-coil formation is shown. The coiled-coil structure was predicted using the COILS program with two different windows. The figure shows the comparison of coiled-coil-forming tendency in a 14-residue window of the C-terminal tail of yeast, human, bovine, and mouse Oxa1. The amino acid listed as zero in the figure corresponds to residues 317, 334, 334, and 330 residues in full-length yeast, human, bovine, and mouse Oxa1, respectively.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Sequencing, Purification, Plasmid Preparation

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Effect of protein concentration, salt, and TFE on the secondary structure of Oxa1L-CTT determined by CD. A, shown is the effect of Oxa1L-CTT concentration (0.1, 0.2, and 0.34 mg/ml) on the CD spectra. B, shown is the effect of salt concentration on the CD spectra of Oxa1L-CTT. The protein concentration was 0.1 mg/ml. C, shown is the effect of TFE concentration on the CD spectra of Oxa1L-CTT. Protein concentration was 0.2 mg/ml.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Protein Concentration, Concentration Assay

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Oligomerization of Oxa1L-CTT. A, shown is the effect of KCl on oligomerization of Oxa1L-CTT as examined by analytical ultracentrifugation. The panels show the representative equilibrium sedimentation profiles at three different KCl concentrations at 10 mm MgCl2. The data are plotted as the absorption of Oxa1L-CTT (0.6 mg/ml) at 280 nm versus the distance from the center of the axis of rotation (radius). The lower section of each panel shows the raw data in closed circles. The lines represent the best fits. The upper panels show the residual for the corresponding given fit. The global fit of three protein concentrations (0.3, 0.6, and 0.9 mg/ml) is not shown. The data presented here were obtained at 24,000 rpm. B, detection of dimer and tetramer formation of Oxa1L-CTT by DMS cross-linking followed by Western blotting as described in “Experimental Procedures” is shown.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Sedimentation, Western Blot

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Interaction of the mammalian mitochondrial large ribosomal subunit (39 S) with Oxa1L-CTT analyzed by surface plasma resonance. A, shown is the RU change of Oxa1L-CTT binding to 39 S (circles) and 28 S (triangles) as a function of Oxa1L-CTT concentrations. Ribosomes (39 S and 28 S) and BSA were immobilized on a L1 sensor chip, and Oxa1L-CTT was flowed through the cell as described under “Experimental Procedures.” The RU values were recorded for each injection after 15 s of buffer exchange. The value of the RU from the cell carrying BSA has been subtracted from each value. The solid circles represent experimental data, and the line represents a sigmoidal fit. B, the salt dependence of the RU change when Oxa1L-CTT (20 μl at 0.18 μm) was used in buffer containing different KCl concentrations and injected at a flow rate of 10 μl/min, and RU values were noted from the base line after 15 s of buffer exchange.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Binding Assay, Injection, Buffer Exchange

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Estimation of the thermodynamic parameters governing the interaction of Oxa1L-CTT with mitochondrial 55 S ribosomes using isothermal titration calorimetry. A, raw data for the binding of Oxa1L-CTT to 55 S ribosomes provided as the power output (μcal/s) as a function of time are shown. The protein concentration was 80 μm (syringe), and the 55 S ribosome concentration was 4 μm (cell). The first injection is only for the purpose of the experimental setup and is ignored for data analysis. B, shown is the amount of heat evolved at each injection normalized to the number of moles of Oxa1L-CTT injected (kcal/mol) versus the molar ratio of Oxa1L-CTT to 55 S ribosome. The solid line represents the nonlinear least squares fit for the data.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Isothermal Titration Calorimetry, Binding Assay, Protein Concentration, Concentration Assay, Injection

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Strategy used to identify ribosomal proteins near the Oxa1L binding site. Oxa1L-CTT was incubated with 39 S subunits and cross-linked to nearby proteins using DMS as described under “Experimental Procedures.” Cross-linked complexes were purified by centrifugation through a sucrose cushion. The ribosomes were then denatured, and ribosomal proteins cross-linked to Oxa1L-CTT were recovered on Ni-NTA. Cross-linked proteins were digested with trypsin, and the proteins present were identified by LC/MS/MS.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Binding Assay, Incubation, Purification, Centrifugation, Liquid Chromatography with Mass Spectroscopy

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: Peptides and ion scores of ribosomal proteins cross-linked to Oxa1L-CTT Ion scores of greater than 35 are considered significant.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Sequencing

Journal: The Journal of Biological Chemistry

Article Title: Properties of the C-terminal Tail of Human Mitochondrial Inner Membrane Protein Oxa1L and Its Interactions with Mammalian Mitochondrial Ribosomes *

doi: 10.1074/jbc.M110.148262

Figure Lengend Snippet: A, structural representation the putative binding site of Oxa1L mapped onto the structure of the Thermus thermophilus 50 S subunit (PDB coordinate 2WRL) using PyMOL. A, shown is a representation of the exit tunnel on bacterial ribosomes showing the traditional proteins (L22, L23, L24, and L29) near to exit tunnel of the 50 S ribosomal subunit. B, shown is a representation of the mammalian mitochondrial ribosomal proteins homologous to bacterial L13, L20, and L28 (space-filled) modeled onto the bacterial 50 S subunit. The regions of the rRNA missing in the mammalian mitochondrial ribosome have been manually removed from the coordinates for the 50 S subunit. In E. coli, L28 is almost completely covered by rRNA, but these segments of rRNA are missing in the 39 S subunit, leaving L28 more exposed to solvent. C, shown is a comparison of the sizes of bacterial and yeast L13, L20, and L28 with mitochondrial homologs. L20 is absent in yeast. The molecular weights of the MRPs are estimated after the removal of import signals predicated by MitoProt II.

Article Snippet: The cDNA clone of human Oxa1L was obtained from American Type Culture Collection (ATCC number 10961183, IMAGE 40017377).

Techniques: Binding Assay

a, Mitochondrial content assessment. Levels of PINK1, a mitophagy marker, TOM20, and VDAC, commonly used mitochondrial markers, were assessed in infected and mock-infected HeLa cells. Whole-cell lysates were analyzed with anti-PINK1, anti-TOM20, and anti-VDAC antibodies. The values were normalized with GAPDH or β-tubulin levels. b, Abundance levels of nine mitochondrial proteins were analyzed in whole-cell lysates obtained from infected and mock-infected HeLa cells. Specific antibodies were used to assess each protein. The values were normalized with β-tubulin or GAPDH levels. c, Abundance levels of CH60, OXA1L, and TIM44 proteins were assessed in biotin-phenol labeled and enriched samples from infected and mock-infected HeLa cells. The samples were prepared simultaneously, and equal amounts were loaded onto the gel. Specific antibodies were used to assess each protein. On all graphs in this figure, the bars represent the normalized means ± s.d. Statistical significance was calculated using a parametric unpaired t-test, *p < 0.05.

Journal: bioRxiv

Article Title: Deep Learning-Driven Discovery of Mitochondrial Factors Modulating Influenza A Virus Infection

doi: 10.64898/2026.02.25.707858

Figure Lengend Snippet: a, Mitochondrial content assessment. Levels of PINK1, a mitophagy marker, TOM20, and VDAC, commonly used mitochondrial markers, were assessed in infected and mock-infected HeLa cells. Whole-cell lysates were analyzed with anti-PINK1, anti-TOM20, and anti-VDAC antibodies. The values were normalized with GAPDH or β-tubulin levels. b, Abundance levels of nine mitochondrial proteins were analyzed in whole-cell lysates obtained from infected and mock-infected HeLa cells. Specific antibodies were used to assess each protein. The values were normalized with β-tubulin or GAPDH levels. c, Abundance levels of CH60, OXA1L, and TIM44 proteins were assessed in biotin-phenol labeled and enriched samples from infected and mock-infected HeLa cells. The samples were prepared simultaneously, and equal amounts were loaded onto the gel. Specific antibodies were used to assess each protein. On all graphs in this figure, the bars represent the normalized means ± s.d. Statistical significance was calculated using a parametric unpaired t-test, *p < 0.05.

Article Snippet: The cells were collected after 48 hours to analyse for knockdown efficiency or used for further experiments. siRNA used: Hsp60 (HSPD1) Human siRNA Oligo Duplex (OriGene, locus ID 3329) AccuTarget Predesigned Human ETHE1 siRNA (Bioneer, locus ID 23474) AccuTarget Predesigned Human GRP75 siRNA (Bioneer, locus ID 3313) LETM1 Human siRNA Oligo Duplex (OriGene, locus ID 3954) AccuTarget Predesigned Human LONP1 siRNA (Bioneer, locus ID 9361) OXA1L Human siRNA Oligo Duplex (OriGene, locus ID 5018) AccuTarget Predesigned Human MPPB siRNA (Bioneer, locus ID 9512) AccuTarget Predesigned Human TIM44 siRNA (Bioneer, locus ID 10469) AccuTarget Predesigned Human SQOR siRNA (Bioneer, locus ID 58472) Non-targeting scramble siRNA (siControl) was purchased from OriGene.

Techniques: Marker, Infection, Labeling

$Abundance levels of CH60, OXA1L and TIM44 proteins were calculated in mitochondrial fractions. The values were normalized with TOM20 levels. The bars on all graphs represent the normalized means ± s.d. of triplicate samples. Statistical significance was calculated using a parametric unpaired t-test, *p < 0.05.$

Journal: bioRxiv

Article Title: Deep Learning-Driven Discovery of Mitochondrial Factors Modulating Influenza A Virus Infection

doi: 10.64898/2026.02.25.707858

Figure Lengend Snippet: Abundance levels of CH60, OXA1L and TIM44 proteins were calculated in mitochondrial fractions. The values were normalized with TOM20 levels. The bars on all graphs represent the normalized means ± s.d. of triplicate samples. Statistical significance was calculated using a parametric unpaired t-test, *p < 0.05.

Techniques:

Fig. 1. Evaluation of immunoreactivities of antibodies against MCU and EMRE. (A), Upper: Domains/motifs of mouse MCU. MTS, mitochondrial transit sequence (Met1-Thr49); NTD, N-terminal domain (Val74-Arg164); CC, coiled-coil domain (Ile191-Arg220 for CC1, Arg310-Gln338 for CC2); TM, transmembrane region (Leu233-Glu256 for TM1, Val265-Val282 for TM2). Schematic representation of epitopes of antibodies against mouse MCU; ABMCU1, ABMCU2, ABMCU3, ABMCU4: the location of each epitope is shown by the bold line. Lower: the mitochondria isolated from mouse brain and HeLa cells (5.0 and 10.0 µglane−1, respectively) were subjected to SDS/PAGE followed by CBB staining and immunoblotting using each MCU antibody. Mature MCU is shown by arrows; the bands formed by nonspeciﬁc reactions of the antibodies are indicated by asterisks. (B), Upper: Domains/motifs of mouse EMRE. MTS, mitochondrial transit sequence (Met1-Ser47); TM, transmembrane region (Phe65-Ile84 for TM). Schematic representation of epitopes of antibodies against mouse EMRE; ABEMRE1 Lower: immunoblots using each EMRE antibody and CBB staining; mature EMRE is shown by the arrow. (C), Immunoblot of the mitochondria isolated from wild-type (WT) HeLa cells, MCU-knockout HeLa cells, and EMRE-knockout HeLa cells (10.0 µglane−1 of each), obtained by using ABMCU1 and ABEMRE2. As a loading control, human OXA1L was detected with anti-OXA1L antibody (Santa Cruz, sc-136011).

Journal: FEBS open bio

Article Title: Quantitative analysis of mitochondrial calcium uniporter (MCU) and essential MCU regulator (EMRE) in mitochondria from mouse tissues and HeLa cells.

doi: 10.1002/2211-5463.13371

Figure Lengend Snippet: Fig. 1. Evaluation of immunoreactivities of antibodies against MCU and EMRE. (A), Upper: Domains/motifs of mouse MCU. MTS, mitochondrial transit sequence (Met1-Thr49); NTD, N-terminal domain (Val74-Arg164); CC, coiled-coil domain (Ile191-Arg220 for CC1, Arg310-Gln338 for CC2); TM, transmembrane region (Leu233-Glu256 for TM1, Val265-Val282 for TM2). Schematic representation of epitopes of antibodies against mouse MCU; ABMCU1, ABMCU2, ABMCU3, ABMCU4: the location of each epitope is shown by the bold line. Lower: the mitochondria isolated from mouse brain and HeLa cells (5.0 and 10.0 µglane−1, respectively) were subjected to SDS/PAGE followed by CBB staining and immunoblotting using each MCU antibody. Mature MCU is shown by arrows; the bands formed by nonspeciﬁc reactions of the antibodies are indicated by asterisks. (B), Upper: Domains/motifs of mouse EMRE. MTS, mitochondrial transit sequence (Met1-Ser47); TM, transmembrane region (Phe65-Ile84 for TM). Schematic representation of epitopes of antibodies against mouse EMRE; ABEMRE1 Lower: immunoblots using each EMRE antibody and CBB staining; mature EMRE is shown by the arrow. (C), Immunoblot of the mitochondria isolated from wild-type (WT) HeLa cells, MCU-knockout HeLa cells, and EMRE-knockout HeLa cells (10.0 µglane−1 of each), obtained by using ABMCU1 and ABEMRE2. As a loading control, human OXA1L was detected with anti-OXA1L antibody (Santa Cruz, sc-136011).

Article Snippet: As a loading control, human OXA1L was detected with anti-OXA1L antibody (Santa Cruz, sc-136011).

Techniques: Sequencing, Isolation, SDS Page, Staining, Western Blot, Knock-Out, Control

Journal: Cell

Article Title: Mitochondrial Protein Synthesis Adapts to Influx of Nuclear-Encoded Protein

doi: 10.1016/j.cell.2016.09.003

Figure Lengend Snippet:

Article Snippet: Mouse monoclonal antibody to human OXA1L , Proteintech , 66128-1.

Techniques: FLAG-tag, Recombinant, cDNA Synthesis, DNA Ligation, Expressing, Plasmid Preparation, Sequencing, Software

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