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domain structure of neurospora proteins  (InterPro Inc)

 
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    InterPro Inc domain structure of neurospora proteins
    Experimental design and results of <t>Neurospora</t> telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate
    Domain Structure Of Neurospora Proteins, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/domain+structure+of+neurospora+proteins/pmc04650311-52-13-17?v=InterPro+Inc
    Average 90 stars, based on 1 article reviews
    domain structure of neurospora proteins - by Bioz Stars, 2026-07
    90/100 stars

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    1) Product Images from "Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats"

    Article Title: Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats

    Journal: BMC Genomics

    doi: 10.1186/s12864-015-2158-0

    Experimental design and results of Neurospora telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate
    Figure Legend Snippet: Experimental design and results of Neurospora telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate

    Techniques Used: Incubation, Control, Sequencing, Mass Spectrometry, Binding Assay

    Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ). The position of the domains and length of the proteins are drawn to scale. b Overview of the corresponding homologs in S. cerevisiae , S. pombe , C. albicans and A. fumigatus as determined by sequence similarity search. The telomeric motifs are indicated for each species. Blast hits in black are true homologs whereas blast hits in white showed weak homology and the reverse blast identified a different homologous protein. The first e-value represents the search of the N. crassa protein vs. the respective species and the second e-value the reverse blast search. N. crassa names in blue are proposed based on experimental data from this study
    Figure Legend Snippet: Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ). The position of the domains and length of the proteins are drawn to scale. b Overview of the corresponding homologs in S. cerevisiae , S. pombe , C. albicans and A. fumigatus as determined by sequence similarity search. The telomeric motifs are indicated for each species. Blast hits in black are true homologs whereas blast hits in white showed weak homology and the reverse blast identified a different homologous protein. The first e-value represents the search of the N. crassa protein vs. the respective species and the second e-value the reverse blast search. N. crassa names in blue are proposed based on experimental data from this study

    Techniques Used: Sequencing

    Characterization of binding mode of Neurospora TTAGGG-binding proteins. a Western blots from pull-downs of recombinantly expressed Neurospora proteins incubated with concatemerized oligonucleotides of telomeric repeats (TTAGGG) or a shuffled control sequence (TGTGAG) to check for direct binding. b Comparative binding test for double-stranded versus single-stranded telomeric DNA. Direct TTAGGG-binding proteins from ( a ) were incubated with increasing amounts of single-stranded TTAGGG repeats. Only NCU2404 binding is decreased at higher ssTTAGGG oligonucleotide concentrations revealing the other 5 proteins as double-strand binders. c Western blot of the competition assay of NCU02404 shows that its binding can only be competed with ssTTAGGG but not with an unrelated control sequence
    Figure Legend Snippet: Characterization of binding mode of Neurospora TTAGGG-binding proteins. a Western blots from pull-downs of recombinantly expressed Neurospora proteins incubated with concatemerized oligonucleotides of telomeric repeats (TTAGGG) or a shuffled control sequence (TGTGAG) to check for direct binding. b Comparative binding test for double-stranded versus single-stranded telomeric DNA. Direct TTAGGG-binding proteins from ( a ) were incubated with increasing amounts of single-stranded TTAGGG repeats. Only NCU2404 binding is decreased at higher ssTTAGGG oligonucleotide concentrations revealing the other 5 proteins as double-strand binders. c Western blot of the competition assay of NCU02404 shows that its binding can only be competed with ssTTAGGG but not with an unrelated control sequence

    Techniques Used: Binding Assay, Western Blot, Incubation, Control, Sequencing, Competitive Binding Assay

    Model for the N. crassa telosome based on our mass spectrometric screen and the binding analysis. Neurospora has at least six double strand binding proteins (five were validated experimentally [ green ] and one was inferred from homology [ grey ]) and two single-strand binding proteins of which we have experimentally validated one [ yellow ] while the other [ grey ] was inferred from homology. Connections indicate homologs between Neurospora and the other yeast species
    Figure Legend Snippet: Model for the N. crassa telosome based on our mass spectrometric screen and the binding analysis. Neurospora has at least six double strand binding proteins (five were validated experimentally [ green ] and one was inferred from homology [ grey ]) and two single-strand binding proteins of which we have experimentally validated one [ yellow ] while the other [ grey ] was inferred from homology. Connections indicate homologs between Neurospora and the other yeast species

    Techniques Used: Binding Assay



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    domain structure of neurospora proteins  (InterPro Inc)
    90
    InterPro Inc domain structure of neurospora proteins
    Experimental design and results of <t>Neurospora</t> telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate
    Domain Structure Of Neurospora Proteins, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/domain+structure+of+neurospora+proteins/pmc04650311-52-13-17?v=InterPro+Inc
    Average 90 stars, based on 1 article reviews
    domain structure of neurospora proteins - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

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    Experimental design and results of Neurospora telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate

    Journal: BMC Genomics

    Article Title: Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats

    doi: 10.1186/s12864-015-2158-0

    Figure Lengend Snippet: Experimental design and results of Neurospora telomere pull-down. a Schematic workflow of the label-free telomere interaction screen. Extracts of N. crassa were incubated with either a telomeric probe (TTAGGG) or a shuffled control sequence (TGTGAG). For each probe, four pull-downs were performed independently and measured using high resolution mass spectrometry. To identify TTAGGG repeat binding proteins the MaxLFQ algorithm was used to compare individual peptide intensities between the telomeric bait and the shuffled control sequence. b Volcano plot of the telosome of N. crassa . We identified 12 proteins (two-sided t -test, Welch, FDR = 0.05) to be enriched at the telomeric TTAGGG probe compared to the shuffled control. c Heatmap representation of z-scored enrichment values obtained from MaxLFQ intensities for the 12 significantly enriched Neurospora proteins validates reproducible binding behaviour in each replicate

    Article Snippet: Fig. 2 Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ).

    Techniques: Incubation, Control, Sequencing, Mass Spectrometry, Binding Assay

    Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ). The position of the domains and length of the proteins are drawn to scale. b Overview of the corresponding homologs in S. cerevisiae , S. pombe , C. albicans and A. fumigatus as determined by sequence similarity search. The telomeric motifs are indicated for each species. Blast hits in black are true homologs whereas blast hits in white showed weak homology and the reverse blast identified a different homologous protein. The first e-value represents the search of the N. crassa protein vs. the respective species and the second e-value the reverse blast search. N. crassa names in blue are proposed based on experimental data from this study

    Journal: BMC Genomics

    Article Title: Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats

    doi: 10.1186/s12864-015-2158-0

    Figure Lengend Snippet: Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ). The position of the domains and length of the proteins are drawn to scale. b Overview of the corresponding homologs in S. cerevisiae , S. pombe , C. albicans and A. fumigatus as determined by sequence similarity search. The telomeric motifs are indicated for each species. Blast hits in black are true homologs whereas blast hits in white showed weak homology and the reverse blast identified a different homologous protein. The first e-value represents the search of the N. crassa protein vs. the respective species and the second e-value the reverse blast search. N. crassa names in blue are proposed based on experimental data from this study

    Article Snippet: Fig. 2 Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ).

    Techniques: Sequencing

    Characterization of binding mode of Neurospora TTAGGG-binding proteins. a Western blots from pull-downs of recombinantly expressed Neurospora proteins incubated with concatemerized oligonucleotides of telomeric repeats (TTAGGG) or a shuffled control sequence (TGTGAG) to check for direct binding. b Comparative binding test for double-stranded versus single-stranded telomeric DNA. Direct TTAGGG-binding proteins from ( a ) were incubated with increasing amounts of single-stranded TTAGGG repeats. Only NCU2404 binding is decreased at higher ssTTAGGG oligonucleotide concentrations revealing the other 5 proteins as double-strand binders. c Western blot of the competition assay of NCU02404 shows that its binding can only be competed with ssTTAGGG but not with an unrelated control sequence

    Journal: BMC Genomics

    Article Title: Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats

    doi: 10.1186/s12864-015-2158-0

    Figure Lengend Snippet: Characterization of binding mode of Neurospora TTAGGG-binding proteins. a Western blots from pull-downs of recombinantly expressed Neurospora proteins incubated with concatemerized oligonucleotides of telomeric repeats (TTAGGG) or a shuffled control sequence (TGTGAG) to check for direct binding. b Comparative binding test for double-stranded versus single-stranded telomeric DNA. Direct TTAGGG-binding proteins from ( a ) were incubated with increasing amounts of single-stranded TTAGGG repeats. Only NCU2404 binding is decreased at higher ssTTAGGG oligonucleotide concentrations revealing the other 5 proteins as double-strand binders. c Western blot of the competition assay of NCU02404 shows that its binding can only be competed with ssTTAGGG but not with an unrelated control sequence

    Article Snippet: Fig. 2 Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ).

    Techniques: Binding Assay, Western Blot, Incubation, Control, Sequencing, Competitive Binding Assay

    Model for the N. crassa telosome based on our mass spectrometric screen and the binding analysis. Neurospora has at least six double strand binding proteins (five were validated experimentally [ green ] and one was inferred from homology [ grey ]) and two single-strand binding proteins of which we have experimentally validated one [ yellow ] while the other [ grey ] was inferred from homology. Connections indicate homologs between Neurospora and the other yeast species

    Journal: BMC Genomics

    Article Title: Identification of TTAGGG-binding proteins in Neurospora crassa , a fungus with vertebrate-like telomere repeats

    doi: 10.1186/s12864-015-2158-0

    Figure Lengend Snippet: Model for the N. crassa telosome based on our mass spectrometric screen and the binding analysis. Neurospora has at least six double strand binding proteins (five were validated experimentally [ green ] and one was inferred from homology [ grey ]) and two single-strand binding proteins of which we have experimentally validated one [ yellow ] while the other [ grey ] was inferred from homology. Connections indicate homologs between Neurospora and the other yeast species

    Article Snippet: Fig. 2 Structure and evolutionary conservation of TTAGGG-associated proteins. a Domain structure of Neurospora proteins reported by InterPro 46.0 ( http://www.ebi.ac.uk/interpro/ ).

    Techniques: Binding Assay