Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation.

ABSTRACT:

Background

Reversible posttranslational protein modifications such as phosphorylation of Ser/Thr/Tyr and Met oxidation are critical for both metabolic regulation and cellular signalling. Although these modifications are typically studied individually, herein we describe the potential for cross-talk and hierarchical regulation.

Results

The proximity of Met to Ser/Thr/Tyr within the proteome has not previously been addressed. In order to consider the possibility of a generalized interaction, we performed a trans-kingdom sequence analysis of known phosphorylation sites in proteins from bacteria, fungi, plants, and animals. The proportion of phosphorylation sites that include a Met within a 13-residue window centered upon Ser/Thr/Tyr is significantly less than the occurrence of

SUBMITTER: Rao R 

PROVIDER: S-EPMC3851202 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature