Towards the entire proteome of the model bacterium Bacillus subtilis by gel-based and gel-free approaches

Wolff, Susanne; Antelmann, Haike; Albrecht, Dirk; Becher, Dörte; Bernhardt, Jörg; Bron, Sierd; Büttner, Knut; Dijl, Jan Maarten van; Eymann, Christine; Otto, Andreas; Tam, Le Thi; Hecker, Michael

doi:10.1016/j.jchromb.2006.09.029

Cited by 59 publications

(51 citation statements)

References 86 publications

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“…In relation to this, with the aim of determining the protein profile of the B. longum envelope, and as a first approach to undertaking deeper functional studies, we analysed different subcellular fractions. The application of gel-based and gel-free technologies, combined with high-throughput techniques, allowed us to identify 218 proteins; about 70 % of them were predicted to be, or were previously described as being, in the cell envelope of Gram-positive bacteria (Antikainen et al, 2007;Candela et al, 2007;Eymann et al, 2004;Granato et al, 2004;Jang & Hanash 2003;Kelly et al, 2005b;Nandakumar et al, 2005;Rivera-Amill et al, 2001;Rodríguez-Ortega et al, 2006;Schaumburg et al, 2004;Severin et al, 2007;Silveira et al, 2004;Tjalsma et al, 2008;Wolff et al, 2007). Furthermore, 48 of them are predicted to be integral membrane proteins (contain hypothetical transmembrane segments) and 30 of them have different extracytoplasmic sorting signals.…”

Section: Discussionmentioning

confidence: 99%

The cell-envelope proteome of Bifidobacterium longum in an in vitro bile environment

et al. 2009

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Host-bacteria interactions are often mediated via surface-associated proteins. The identification of these proteins is an important goal of bacterial proteomics. To address how bile can influence the cell-envelope proteome of Bifidobacterium longum biotype longum NCIMB 8809, we analysed its membrane protein fraction using stable isotope labelling of amino acids in cell culture (SILAC). We were able to identify 141 proteins in the membrane fraction, including a large percentage of the theoretical transporters of this species. Moreover, the envelope-associated soluble fraction was analysed using different subfractionation techniques and differential in-gel fluorescence electrophoresis (DIGE). This approach identified 128 different proteins. Some of them were well-known cell wall proteins, but others were highly conserved cytoplasmic proteins probably displaying a 'moonlighting' function. We were able to identify 11 proteins in the membrane fraction and 6 proteins in the envelope-associated soluble fraction whose concentration varied in the presence of bile. Bile promoted changes in the levels of proteins with important biological functions, such as some ribosomal proteins and enolase. Also, oligopeptide-binding proteins were accumulated on the cell surface, which was reflected in a different tripeptide transport rate in the cells grown with bile. The data reported here will provide the first cell-envelope proteome map for B. longum, and may contribute to understanding the bile tolerance of these bacteria

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Section: Discussionmentioning

confidence: 99%

The cell-envelope proteome of Bifidobacterium longum in an in vitro bile environment

et al. 2009

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“…Though we can look back on 25 years of proteome research in B. subtilis (Streips et al, 1985;Richter et al, 1986;Wolff et al, 2007), still one-third of B. subtilis 4100 genes are not assigned to a defined function yet (Sonenshein et al, 2001), and only for about one-third of all genes the corresponding protein could be demonstrated so far (Wolff et al, 2007).…”

Section: Proteome Of the Model Bacterium B Subtilismentioning

confidence: 99%

“…Therefore, two major classes of proteomes have to be defined: the proteome of growing cells (vegetative proteome) and the proteome of non-growing cells suffering from stress or starvation (Wolff et al, 2007) …”

Section: Proteome Of the Model Bacterium B Subtilismentioning

confidence: 99%

“…subtilis proteome, are not covered by conventional 2D-PAGE (pI 4-7) (Wolff et al, 2007). A gel-free approach, in which the cytosolic proteome fraction of growing B.…”

Section: Cytosolic Proteome Map Of Growing Cellsmentioning

confidence: 99%

“…There are also proteins smaller than 10 kDa or larger than 100 kDa which will probably bottom out the gel or will not migrate into the 2D-gel, respectively. Despite the high-resolution power of 2D-PAGE one can not rule out that some proteins could not be identified from the gel due to protein comigration, which results in masking of small protein spots by higher abundant proteins (Wolff et al, 2007).…”

Section: Cytosolic Proteome Map Of Growing Cellsmentioning

confidence: 99%

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