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Volumn 8, Issue 3, 1998, Pages 393-400

Identifying proteins and post-translational modifications by mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; REVIEW;

EID: 0032102792     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80075-4     Document Type: Article
Times cited : (94)

References (63)
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    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
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    • Rapid protein sequencing by tandem mass spectrometry and cDNA cloning of p20-CGGBP. A novel protein that binds to the unstable triplet repeat 5′-d(CGG)n-3′ in the human FMR1 gene
    • of special interest. This study illustrates that mass spectrometric peptide sequencing can provide a short cut to interesting genes. Searching of EST databases using peptide sequence tags identified a clone containing the full-length coding sequence of a hitherto unknown protein. This allowed the rapid cloning of the cognate gene. Given the tremendous growth of EST databases, this strategy is expected to become more generally applicable in the future.
    • Deissler H, Wilm M, Gene B, Schmitz B, Ternes T, Naumann F, Mann M, Doerfler W. Rapid protein sequencing by tandem mass spectrometry and cDNA cloning of p20-CGGBP. A novel protein that binds to the unstable triplet repeat 5′-d(CGG)n-3′ in the human FMR1 gene. of special interest J Biol Chem. 272:1997;16761-16768 This study illustrates that mass spectrometric peptide sequencing can provide a short cut to interesting genes. Searching of EST databases using peptide sequence tags identified a clone containing the full-length coding sequence of a hitherto unknown protein. This allowed the rapid cloning of the cognate gene. Given the tremendous growth of EST databases, this strategy is expected to become more generally applicable in the future.
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    • Reverse transcriptase motifs in the catalytic subunit of telomerase
    • of outstanding interest. Tandem mass spectrometric de novo sequencing of multiple peptides of low picomole amounts of the catalytic subunit of telomerase allowed the generation of degenerate oligonucleotide primers for the subsequent cloning of the corresponding gene. More than 150 amino acids were represented in respective MS/MS spectra. Detailed sequence analysis of the cloned gene revealed that telomerase contains reverse transcriptase motifs that were found to be essential for chromosome replication. This paper represents the first instance of the cloning of a novel protein of major biological significance using MS data from sample amounts too low for traditional sequencing strategies.
    • Lingner J, Hughes TR, Shevchenko A, Mann M, Lundblad V, Cech TR. Reverse transcriptase motifs in the catalytic subunit of telomerase. of outstanding interest Science. 276:1997;561-567 Tandem mass spectrometric de novo sequencing of multiple peptides of low picomole amounts of the catalytic subunit of telomerase allowed the generation of degenerate oligonucleotide primers for the subsequent cloning of the corresponding gene. More than 150 amino acids were represented in respective MS/MS spectra. Detailed sequence analysis of the cloned gene revealed that telomerase contains reverse transcriptase motifs that were found to be essential for chromosome replication. This paper represents the first instance of the cloning of a novel protein of major biological significance using MS data from sample amounts too low for traditional sequencing strategies.
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    • Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry
    • of special interest. This study represents the first report on the identification of members of an entire multiprotein complex by mass spectrometry. All previously known members of the complex were identified by peptide sequence tags following immunoaffinity chromatography and SDS-PAGE. Four additional proteins were identified and subsequently shown to play a role within the protein complex.
    • Neubauer G, Gottschalk A, Fabrizio P, Seraphin B, Luhrmann R, Mann M. Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry. of special interest Proc Natl Acad Sci. 94:1997;385-390 This study represents the first report on the identification of members of an entire multiprotein complex by mass spectrometry. All previously known members of the complex were identified by peptide sequence tags following immunoaffinity chromatography and SDS-PAGE. Four additional proteins were identified and subsequently shown to play a role within the protein complex.
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    • of special interest. LC/MS/MS was used as the exclusive tool for the identification of proteins from Haemophilus influenzae that were separated by 2D gels. Automatic LC/MS/MS enabled the analysis of 300 out of a total of 400 protein spots, at a rate of 22 proteins per day. Several proteins that were not annotated in the genomic sequence were identified in this study. See also [49].
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