Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 421575
Title Effect of acid stress on protein expression and phosphorylation in Lactobacillus rhamnosus GG
Author(s) Koponen, J.; Laakso, K.; Koskenniemi, K.; Kankainen, M.; Savijoki, K.; Nyman, T.A.; Vos, W.M. de; Tynkkynen, S.; Kalkkinen, N.; Varmanen, P.
Source Journal of Proteomics 75 (2012)4. - ISSN 1874-3919 - p. 1357 - 1374.
DOI http://dx.doi.org/10.1016/j.jprot.2011.11.009
Department(s) Microbiological Laboratory
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) gram-positive bacteria - low-ph - lactococcus-lactis - proteomic analysis - bacillus-subtilis - heat-shock - ser/thr/tyr phosphoproteome - tolerance response - probiotic bacteria - mass-spectrometry
Abstract Acidic environments encountered in food products and during gastrointestinal tract passage affect the survival of bacteria that are marketed as probiotics. In this study, the global proteome responses of the probiotic lactic acid bacterium Lactobacillus rhamnosus GG to two physiologically relevant pH conditions (pH 4.8 and pH 5.8) were studied by 2-D DIGE. The proteomics data were complemented with transcriptome analyses by whole-genome DNA microarrays. The cells were cultured in industrial-type whey medium under strictly defined bioreactor conditions. In total, 2-D DIGE revealed the pH-dependent formation of 92 protein spots. In response to lower pH conditions, the strongest up-regulation of all proteins was detected for a predicted surface antigen, LGG_02016. In addition, the acid pH was found to up-regulate the expression of F(0)F(1)-ATP synthase genes whereas the abundance of proteins participating in nucleotide biosynthesis and protein synthesis was significantly diminished. Moreover, the results suggest that L. rhamnosus GG modulates its pyruvate metabolism depending on the growth pH. Furthermore, a growth pH-dependent protein phosphorylation phenomenon was detected in several L. rhamnosus GG proteins with ProQ Diamond 2-DE gel staining. Proteins participating in central cellular pathways were shown to be phosphorylated, and the phosphorylation of glycolytic enzymes was found to be especially extensive
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