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Physical and computational analysis of the yeast Kluyveromyces lactis secreted proteome
Author(s) -
Swaim Catherine L.,
Anton Brian P.,
Sharma Shamik S.,
Taron Christopher H.,
Benner Jack S.
Publication year - 2008
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.200700764
Subject(s) - kluyveromyces lactis , kluyveromyces , proteome , secretory protein , in silico , biology , yeast , secretion , proteomics , heterologous , biochemistry , proteolysis , saccharomyces cerevisiae , microbiology and biotechnology , computational biology , gene , enzyme
Secretion of proteins is the most common approach to protein expression in Kluyveromyces lactis . A proteomic analysis was performed on spent fermentation medium following bioreactor propagation of a wild‐type industrial strain to identify proteins naturally secreted by K. lactis cells. Multidimensional separations were conducted and RP online ESI‐MS/MS analysis identified 81 secreted proteins. In addition, an in silico analysis predicted 178 K. lactis proteins to be secreted via the general secretory pathway (GSP). These two datasets were compared and approximately 70% of the K. lactis proteins detected in the culture medium possessed a GSP sequence. The detected proteins included those involved with cell wall structure and synthesis, carbohydrate metabolism, and proteolysis, a result that may have significant bearing on heterologous protein expression. Additionally, both the experimental and in silico datasets were compared to similar, previously published datasets for Candida albicans . With the methodology presented here, we provide the deepest penetration into a yeast secretome yet reported.

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