RT Journal Article
SR Electronic
T1 Protein Deacetylase CobB Interplays with c-di-GMP
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 362293
DO 10.1101/362293
A1 Zhaowei Xu
A1 Hainan Zhang
A1 Xingrun Zhang
A1 Chengxi Liu
A1 Hewei Jiang
A1 Fanlin Wu
A1 Lili Qian
A1 Daniel M. Czajkowsky
A1 Shujuan Guo
A1 Lijun Bi
A1 Shihua Wang
A1 Haitao Li
A1 Minjia Tan
A1 Lei Feng
A1 Jingli Hou
A1 Sheng-ce Tao
YR 2018
UL http://biorxiv.org/content/early/2018/07/04/362293.abstract
AB As a ubiquitous bacterial secondary messenger, c-di-GMP plays key regulatory roles in processes such as bacterial motility and transcription regulation. CobB is the Sir2 family protein deacetylase that controls energy metabolism, chemotaxis and DNA supercoiling in many bacteria. Using an E.coli proteome microarray, we found that c-di-GMP strongly binds to CobB. Protein deacetylation assays showed that c-di-GMP inhibits CobB activity and thereby modulates the biogenesis of acetyl-CoA. Through mutagenesis studies, residues R8, R17 and E21 of CobB were shown to be required for c-di-GMP binding. Next, we found that CobB is an effective deacetylase of YdeH, a major diguanylate cyclase (DGC) of E.coli that is endogenously acetylated. Mass spectrometry analysis identified YdeH K4 as the major site of acetylation, and it could be deacetylated by CobB. Interestingly, deacetylation of YdeH enhances its stability and cyclase activity in c-di-GMP production. Thus, our work establishes a novel negative feedback loop linking c-di-GMP biogenesis and CobB-mediated protein deacetylation.