The low molecular weight proteome of Halobacterium salinarum

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Journal of Proteome Research, Vol. 6, No. 4, 2007, p. 1510-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Klein, C, Aivaliotis, M, Olsen, JV, Falb, M, Besir, H, Scheffer, B, Bisle, B, Tebbe, A, Konstantinidis, K, Siedler, F, Pfeiffer, F, Mann, M & Oesterhelt, D 2007, 'The low molecular weight proteome of Halobacterium salinarum', Journal of Proteome Research, vol. 6, no. 4, pp. 1510-8. https://doi.org/10.1021/pr060634q

APA

Klein, C., Aivaliotis, M., Olsen, J. V., Falb, M., Besir, H., Scheffer, B., Bisle, B., Tebbe, A., Konstantinidis, K., Siedler, F., Pfeiffer, F., Mann, M., & Oesterhelt, D. (2007). The low molecular weight proteome of Halobacterium salinarum. Journal of Proteome Research, 6(4), 1510-8. https://doi.org/10.1021/pr060634q

Vancouver

Klein C, Aivaliotis M, Olsen JV, Falb M, Besir H, Scheffer B et al. The low molecular weight proteome of Halobacterium salinarum. Journal of Proteome Research. 2007;6(4):1510-8. https://doi.org/10.1021/pr060634q

Author

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. / The low molecular weight proteome of Halobacterium salinarum. In: Journal of Proteome Research. 2007 ; Vol. 6, No. 4. pp. 1510-8.

Bibtex

@article{ed49e22f2e854f9e98766faaa052ee4e,
title = "The low molecular weight proteome of Halobacterium salinarum",
abstract = "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.",
author = "Christian Klein and Michalis Aivaliotis and Olsen, {Jesper Velgaard} and Michaela Falb and H{\"u}seyin Besir and Beatrix Scheffer and Birgit Bisle and Andreas Tebbe and Kosta Konstantinidis and Frank Siedler and Friedhelm Pfeiffer and Matthias Mann and Dieter Oesterhelt",
note = "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",
year = "2007",
doi = "10.1021/pr060634q",
language = "English",
volume = "6",
pages = "1510--8",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "4",

}

RIS

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