Differential protein phosphorylation-dephosphorylation in response to carbon source in Ruminococcus flavefaciens FD-1

Journal of Applied Microbiology
P E VercoeB A White

Abstract

The aims of this study were to study the effect of cellobiose or cellulose as a carbon source on the differential protein phosphorylation-dephosphorylation of cytoplasmic and membrane-associated proteins from Ruminococcus flavefaciens FD-1. SDS-PAGE analysis was used to compare in vitro labelled proteins (32P-ATP) isolated from R. flavefaciens FD-1 grown on either cellobiose or cellulose as the carbon source. Distinctly different protein phosphorylation patterns were detected depending on carbon source and cell fraction. Analysis of the nature of the phosphorylated proteins indicates that phosphorylated proteins from cellobiose grown cultures are phosphorylated on serine residues, whereas phosphorylated proteins from cellulose grown cultures are phosphorylated on threonine residues. The results of this comparative analysis show a shift from serine phosphorylation of proteins to a threonine phosphorylation when R. flavefaciens FD-1 cells are grown on cellulose as opposed to cellobiose. There appears to be a role for these phosphorylation events in sensing the carbon source for growth and regulating co-ordinated metabolism in R. flavefaciens FD-1. We have demonstrated that there is a protein phosphorylation system in R. flavefaci...Continue Reading

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Citations

Oct 23, 2018·International Journal of Genomics·Renato Graciano de PaulaRoberto Nascimento Silva

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