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t denticola genomic dna  (ATCC)


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    Structured Review

    ATCC t denticola genomic dna
    T Denticola Genomic Dna, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/t+denticola+genomic+dna/Genomic+DNA+from+Treponema+denticola+strain+a/pm41222288-266-16-25
    Average 90 stars, based on 18 article reviews
    t denticola genomic dna - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Mutagenesis:

    Article Title: Transcription regulator TrtA modulates oxygen stress response in Treponema denticola .
    Article Snippet: .. Detection of the mutation in the genome of the wild-type strain and the trtA-deletion mutant of T. denticola Genomic DNA was isolated from T. denticola ATCC 35405 P(−) and T. denticola YK7 as previously described (70). .. A sequence library was constructed from 100 ng of genomic DNA using Illumina DNA Prep (M) Tagmentation kit (Illumina) according to the manufacturer’s instructions.

    Isolation:

    Article Title: Transcription regulator TrtA modulates oxygen stress response in Treponema denticola .
    Article Snippet: .. Detection of the mutation in the genome of the wild-type strain and the trtA-deletion mutant of T. denticola Genomic DNA was isolated from T. denticola ATCC 35405 P(−) and T. denticola YK7 as previously described (70). .. A sequence library was constructed from 100 ng of genomic DNA using Illumina DNA Prep (M) Tagmentation kit (Illumina) according to the manufacturer’s instructions.



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    ATCC t denticola atcc 35405 t genomic dna
    Domain structure and conserved motifs within <t>Treponema</t> <t>denticola</t> encoding putative small alarmone synthetase (Tde-SAS). (A) Schematic diagram showing the domain structure and conserved motifs present within Tde-SAS and Tde-SAS 1–246 (N-terminal catalytic domain). (B) Sequence alignment of the four tetratricopeptide repeat (TPR) motifs (TPR1 to TPR4) in the C-terminal TPR domain of Tde-SAS, indicating their respective start and end positions, as identified by TPRpred . (C) Predicted structural arrangement of the four TPR motifs within the Tde-SAS TPR domain (prepared using SwissModel ). The tandem array of four TPR motifs generates a right-handed superhelical structure, with the region immediately C-terminal to TPR4 (colored dark orange/red) forming an extended α-helix. (D) Multiple sequence alignment of the catalytic domain of Tde-SAS (residues 1 to 228 shown) with diverse SAS proteins: C. glutamicum RelS (RelS Cg ; CgRelS), S. aureus RelP/SAS2 (SaRelP), B. subtilis RelP/Ywac/SAS2 (BsRelP), S. aureus RelQ/SAS1 (SaRelQ), and B. subtilis RelQ/YjbM/SAS1 (BsRelQ). The four respective “synthesis” Syn motifs (Syn1 to Syn4) are indicated with brackets. The figure was prepared using ESPript 3.0 .
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    Thermo Fisher t denticola 33520 genomic dna
    The top line in each row shows the predicted amino acid sequence for HlyA [28]. The second line in each row shows the predicted amino acid sequence encoded by gene hlyB, which is called SEQF1865_00956 in the <t>genomic</t> <t>DNA</t> sequence of T. denticola strain 33520 [http://www.homd.org/index.php]. The asterisks represent amino acids that are identical in the two proteins. The five filled rectangles (▮) mark the residues that have a direct role in the catalysis of cysteine to H2S in HlyA [32,56,57]. Triangles (▼) mark the other eight residues that are also in the active site of T. denticola HlyA [32].
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    ATCC t denticola atcc 35405 genomic dna
    The top line in each row shows the predicted amino acid sequence for HlyA [28]. The second line in each row shows the predicted amino acid sequence encoded by gene hlyB, which is called SEQF1865_00956 in the <t>genomic</t> <t>DNA</t> sequence of T. denticola strain 33520 [http://www.homd.org/index.php]. The asterisks represent amino acids that are identical in the two proteins. The five filled rectangles (▮) mark the residues that have a direct role in the catalysis of cysteine to H2S in HlyA [32,56,57]. Triangles (▼) mark the other eight residues that are also in the active site of T. denticola HlyA [32].
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    DSMZ t denticola dsm14222 genomic dna
    The top line in each row shows the predicted amino acid sequence for HlyA [28]. The second line in each row shows the predicted amino acid sequence encoded by gene hlyB, which is called SEQF1865_00956 in the <t>genomic</t> <t>DNA</t> sequence of T. denticola strain 33520 [http://www.homd.org/index.php]. The asterisks represent amino acids that are identical in the two proteins. The five filled rectangles (▮) mark the residues that have a direct role in the catalysis of cysteine to H2S in HlyA [32,56,57]. Triangles (▼) mark the other eight residues that are also in the active site of T. denticola HlyA [32].
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    Image Search Results


    Domain structure and conserved motifs within Treponema denticola encoding putative small alarmone synthetase (Tde-SAS). (A) Schematic diagram showing the domain structure and conserved motifs present within Tde-SAS and Tde-SAS 1–246 (N-terminal catalytic domain). (B) Sequence alignment of the four tetratricopeptide repeat (TPR) motifs (TPR1 to TPR4) in the C-terminal TPR domain of Tde-SAS, indicating their respective start and end positions, as identified by TPRpred . (C) Predicted structural arrangement of the four TPR motifs within the Tde-SAS TPR domain (prepared using SwissModel ). The tandem array of four TPR motifs generates a right-handed superhelical structure, with the region immediately C-terminal to TPR4 (colored dark orange/red) forming an extended α-helix. (D) Multiple sequence alignment of the catalytic domain of Tde-SAS (residues 1 to 228 shown) with diverse SAS proteins: C. glutamicum RelS (RelS Cg ; CgRelS), S. aureus RelP/SAS2 (SaRelP), B. subtilis RelP/Ywac/SAS2 (BsRelP), S. aureus RelQ/SAS1 (SaRelQ), and B. subtilis RelQ/YjbM/SAS1 (BsRelQ). The four respective “synthesis” Syn motifs (Syn1 to Syn4) are indicated with brackets. The figure was prepared using ESPript 3.0 .

    Journal: Microbiology Spectrum

    Article Title: Functional Characterization of Small Alarmone Synthetase and Small Alarmone Hydrolase Proteins from Treponema denticola

    doi: 10.1128/spectrum.05100-22

    Figure Lengend Snippet: Domain structure and conserved motifs within Treponema denticola encoding putative small alarmone synthetase (Tde-SAS). (A) Schematic diagram showing the domain structure and conserved motifs present within Tde-SAS and Tde-SAS 1–246 (N-terminal catalytic domain). (B) Sequence alignment of the four tetratricopeptide repeat (TPR) motifs (TPR1 to TPR4) in the C-terminal TPR domain of Tde-SAS, indicating their respective start and end positions, as identified by TPRpred . (C) Predicted structural arrangement of the four TPR motifs within the Tde-SAS TPR domain (prepared using SwissModel ). The tandem array of four TPR motifs generates a right-handed superhelical structure, with the region immediately C-terminal to TPR4 (colored dark orange/red) forming an extended α-helix. (D) Multiple sequence alignment of the catalytic domain of Tde-SAS (residues 1 to 228 shown) with diverse SAS proteins: C. glutamicum RelS (RelS Cg ; CgRelS), S. aureus RelP/SAS2 (SaRelP), B. subtilis RelP/Ywac/SAS2 (BsRelP), S. aureus RelQ/SAS1 (SaRelQ), and B. subtilis RelQ/YjbM/SAS1 (BsRelQ). The four respective “synthesis” Syn motifs (Syn1 to Syn4) are indicated with brackets. The figure was prepared using ESPript 3.0 .

    Article Snippet: The Tde-SAS (TDE_RS08190, formerly TDE1711) and Tde-SAH (TDE_RS08100, formerly TDE1690) genes were PCR amplified from T. denticola ATCC 35405 T genomic DNA and cloned into pET28a (+) (Novagen, Merck Millipore) via BamHI/XhoI to create plasmids pET28a-Tde-SAS and pET28a-Tde-SAH, respectively (Table S1).

    Techniques: Sequencing

    The top line in each row shows the predicted amino acid sequence for HlyA [28]. The second line in each row shows the predicted amino acid sequence encoded by gene hlyB, which is called SEQF1865_00956 in the genomic DNA sequence of T. denticola strain 33520 [http://www.homd.org/index.php]. The asterisks represent amino acids that are identical in the two proteins. The five filled rectangles (▮) mark the residues that have a direct role in the catalysis of cysteine to H2S in HlyA [32,56,57]. Triangles (▼) mark the other eight residues that are also in the active site of T. denticola HlyA [32].

    Journal: Anaerobe

    Article Title: Multiple Enzymes Can Make Hydrogen Sulfide From Cysteine in Treponema denticola

    doi: 10.1016/j.anaerobe.2020.102231

    Figure Lengend Snippet: The top line in each row shows the predicted amino acid sequence for HlyA [28]. The second line in each row shows the predicted amino acid sequence encoded by gene hlyB, which is called SEQF1865_00956 in the genomic DNA sequence of T. denticola strain 33520 [http://www.homd.org/index.php]. The asterisks represent amino acids that are identical in the two proteins. The five filled rectangles (▮) mark the residues that have a direct role in the catalysis of cysteine to H2S in HlyA [32,56,57]. Triangles (▼) mark the other eight residues that are also in the active site of T. denticola HlyA [32].

    Article Snippet: With T. denticola 33520 genomic DNA as template, a 1.187 kb fragment was amplified by PCR and ligated into the BamH I/ EcoR I sites of the expression vector pRSET-B (ThermoFisher Scientific).

    Techniques: Sequencing