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The cytosolic, cell surface and extracellular proteomes of the biotechnologically important soil bacterium Corynebacterium efficiens YS‐314 in comparison to those of Corynebacterium glutamicum ATCC 13032
Author(s) -
Hansmeier Nicole,
Chao TzuChiao,
Pühler Alfred,
Tauch Andreas,
Kalinowski Jörn
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500144
Subject(s) - proteome , corynebacterium glutamicum , corynebacterium , biochemistry , proteomics , biology , bacteria , cytosol , extracellular , amino acid , microbiology and biotechnology , chemistry , enzyme , gene , genetics
Reference maps of the cytosolic, cell surface and extracellular proteome fractions of the amino acid‐producing soil bacterium Corynebacterium efficiens YS‐314 were established. The analysis window covers a p I range from 3 to 7 along with a molecular mass range from 10 to 130 kDa. After second‐dimensional separation on SDS‐PAGE and Coomassie staining, computational analysis detected 635 protein spots in the cytosolic proteome fraction, whereas 76 and 102 spots were detected in the cell surface and extracellular proteomes, respectively. By means of MALDI‐TOF‐MS and tryptic peptide mass fingerprinting, 164 cytosolic proteins, 49 proteins of the cell surface and 89 extracellular protein spots were identified, representing in total 177 different proteins. Additionally, reference maps of the three cellular proteome fractions of the close phylogenetic relative Corynebacterium glutamicum ATCC 13032 were generated and used for comparative proteomics. Classification according to the Clusters of Orthologous Groups of proteins scheme and abundance analysis of the identified proteins revealed species‐specific differences. The high abundance of molecular chaperones and amino acid biosynthesis enzymes in C. efficiens points to environmental adaptations of this recently discovered amino acid‐producing bacterium.

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