Diverse and divergent protein post-translational modifications in two growth stages of a natural microbial community

Zhou Li, Yingfeng Wang, Qiuming Yao, Nicholas B. Justice, Tae-Hyuk Ahn, Dong Xu, Robert L. Hettich, Jillian F. Banfield () and Chongle Pan ()
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Zhou Li: Oak Ridge National Laboratory
Yingfeng Wang: Oak Ridge National Laboratory
Qiuming Yao: University of Missouri
Nicholas B. Justice: University of California
Tae-Hyuk Ahn: Oak Ridge National Laboratory
Dong Xu: University of Missouri
Robert L. Hettich: Oak Ridge National Laboratory
Jillian F. Banfield: University of California
Chongle Pan: Oak Ridge National Laboratory

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Detailed characterization of post-translational modifications (PTMs) of proteins in microbial communities remains a significant challenge. Here we directly identify and quantify a broad range of PTMs (hydroxylation, methylation, citrullination, acetylation, phosphorylation, methylthiolation, S-nitrosylation and nitration) in a natural microbial community from an acid mine drainage site. Approximately 29% of the identified proteins of the dominant Leptospirillum group II bacteria are modified, and 43% of modified proteins carry multiple PTM types. Most PTM events, except S-nitrosylations, have low fractional occupancy. Notably, PTM events are detected on Cas proteins involved in antiviral defense, an aspect of Cas biochemistry not considered previously. Further, Cas PTM profiles from Leptospirillum group II differ in early versus mature biofilms. PTM patterns are divergent on orthologues of two closely related, but ecologically differentiated, Leptospirillum group II bacteria. Our results highlight the prevalence and dynamics of PTMs of proteins, with potential significance for ecological adaptation and microbial evolution.

Date: 2014
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DOI: 10.1038/ncomms5405

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