The low molecular weight proteome of Halobacterium salinarum
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The low molecular weight proteome of Halobacterium salinarum. / Klein, Christian; Aivaliotis, Michalis; Olsen, Jesper Velgaard; Falb, Michaela; Besir, Hüseyin; Scheffer, Beatrix; Bisle, Birgit; Tebbe, Andreas; Konstantinidis, Kosta; Siedler, Frank; Pfeiffer, Friedhelm; Mann, Matthias; Oesterhelt, Dieter.
I: Journal of Proteome Research, Bind 6, Nr. 4, 2007, s. 1510-8.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - The low molecular weight proteome of Halobacterium salinarum
AU - Klein, Christian
AU - Aivaliotis, Michalis
AU - Olsen, Jesper Velgaard
AU - Falb, Michaela
AU - Besir, Hüseyin
AU - Scheffer, Beatrix
AU - Bisle, Birgit
AU - Tebbe, Andreas
AU - Konstantinidis, Kosta
AU - Siedler, Frank
AU - Pfeiffer, Friedhelm
AU - Mann, Matthias
AU - Oesterhelt, Dieter
N1 - Keywords: Amino Acid Sequence; Archaeal Proteins; Codon; Electrophoresis, Polyacrylamide Gel; Glycine; Halobacterium salinarum; Molecular Sequence Data; Molecular Weight; Proteome; RNA-Binding Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transcription Factors
PY - 2007
Y1 - 2007
N2 - Systematic investigation of low molecular weight proteins (LMW, below 20 kDa) in the archaeon Halobacterium salinarum resulted in a 6-fold enhancement of the identification rate, reaching 35% of the theoretical proteome in that size range. This was achieved by optimization of common protocols for protein analysis with general applicability. LMW proteins were rapidly and effectively enriched by filter membrane centrifugation followed by tricine SDS-PAGE. Without staining and with significantly shortened digestion protocols, LMW proteins were identified using an FT-ICR mass spectrometer which allows reliable protein identification by MS3 of a single peptide. In addition to a series of technical challenges, small proteins may show low gene expression levels as suggested by their low average codon adaptation index. Twenty functionally uncharacterized proteins contain a characteristic DNA/RNA binding zinc finger motif which underlines the biological relevance of the small proteome and the necessity of their analysis for systems biology.
AB - Systematic investigation of low molecular weight proteins (LMW, below 20 kDa) in the archaeon Halobacterium salinarum resulted in a 6-fold enhancement of the identification rate, reaching 35% of the theoretical proteome in that size range. This was achieved by optimization of common protocols for protein analysis with general applicability. LMW proteins were rapidly and effectively enriched by filter membrane centrifugation followed by tricine SDS-PAGE. Without staining and with significantly shortened digestion protocols, LMW proteins were identified using an FT-ICR mass spectrometer which allows reliable protein identification by MS3 of a single peptide. In addition to a series of technical challenges, small proteins may show low gene expression levels as suggested by their low average codon adaptation index. Twenty functionally uncharacterized proteins contain a characteristic DNA/RNA binding zinc finger motif which underlines the biological relevance of the small proteome and the necessity of their analysis for systems biology.
U2 - 10.1021/pr060634q
DO - 10.1021/pr060634q
M3 - Journal article
VL - 6
SP - 1510
EP - 1518
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 4
ER -
ID: 46461993