Interplay between the bacterial protein deacetylase CobB and the second messenger c‐di‐GMP. (16th August 2019)
- Record Type:
- Journal Article
- Title:
- Interplay between the bacterial protein deacetylase CobB and the second messenger c‐di‐GMP. (16th August 2019)
- Main Title:
- Interplay between the bacterial protein deacetylase CobB and the second messenger c‐di‐GMP
- Authors:
- Xu, Zhaowei
Zhang, Hainan
Zhang, Xingrun
Jiang, Hewei
Liu, Chengxi
Wu, Fanlin
Qian, Lili
Hao, Bingbing
Czajkowsky, Daniel M
Guo, Shujuan
Xu, Zhijing
Bi, Lijun
Wang, Shihua
Li, Haitao
Tan, Minjia
Yan, Wei
Feng, Lei
Hou, Jingli
Tao, Sheng‐ce - Abstract:
- Abstract: 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 Escherichia coli proteome microarray, we found that c‐di‐GMP strongly binds to CobB. Further, protein deacetylation assays showed that c‐di‐GMP inhibits the activity of CobB and thereby modulates the biogenesis of acetyl‐CoA. Interestingly, we also found that one of the key enzymes directly involved in c‐di‐GMP production, DgcZ, is a substrate of CobB. Deacetylation of DgcZ by CobB enhances its activity and thus the production of c‐di‐GMP. Our work establishes a novel negative feedback loop linking c‐di‐GMP biogenesis and CobB‐mediated protein deacetylation. Synopsis: The bacterial secondary messenger c‐di‐GMP plays key regulatory roles in processes such as bacterial motility and transcription regulation. This study reveals a negative feedback loop between c‐di‐GMP biogenesis and CobB‐dependent protein deacetylation. An Escherichia coli proteome‐wide microarray identifies deacetylase CobB as a c‐di‐GMP‐binding protein. c‐di‐GMP binding inhibits deacetylase activity of CobB. CobB deacetylates and activates diguanylate cyclase DgcZ. DgcZ deacetylation promotes c‐di‐GMP production. Abstract : A negative feedback loop between c‐di‐GMP production and the Escherichia coli Sir2‐familyAbstract: 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 Escherichia coli proteome microarray, we found that c‐di‐GMP strongly binds to CobB. Further, protein deacetylation assays showed that c‐di‐GMP inhibits the activity of CobB and thereby modulates the biogenesis of acetyl‐CoA. Interestingly, we also found that one of the key enzymes directly involved in c‐di‐GMP production, DgcZ, is a substrate of CobB. Deacetylation of DgcZ by CobB enhances its activity and thus the production of c‐di‐GMP. Our work establishes a novel negative feedback loop linking c‐di‐GMP biogenesis and CobB‐mediated protein deacetylation. Synopsis: The bacterial secondary messenger c‐di‐GMP plays key regulatory roles in processes such as bacterial motility and transcription regulation. This study reveals a negative feedback loop between c‐di‐GMP biogenesis and CobB‐dependent protein deacetylation. An Escherichia coli proteome‐wide microarray identifies deacetylase CobB as a c‐di‐GMP‐binding protein. c‐di‐GMP binding inhibits deacetylase activity of CobB. CobB deacetylates and activates diguanylate cyclase DgcZ. DgcZ deacetylation promotes c‐di‐GMP production. Abstract : A negative feedback loop between c‐di‐GMP production and the Escherichia coli Sir2‐family deacetylase CobB modulates biogenesis of acetyl‐CoA. … (more)
- Is Part Of:
- EMBO journal. Volume 38:Number 18(2019)
- Journal:
- EMBO journal
- Issue:
- Volume 38:Number 18(2019)
- Issue Display:
- Volume 38, Issue 18 (2019)
- Year:
- 2019
- Volume:
- 38
- Issue:
- 18
- Issue Sort Value:
- 2019-0038-0018-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2019-08-16
- Subjects:
- c‐di‐GMP -- CobB -- diguanylate cyclase -- negative feedback loop -- protein acetylation
Molecular biology -- Periodicals
572.805 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.15252/embj.2018100948 ↗
- Languages:
- English
- ISSNs:
- 0261-4189
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3733.085000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 18717.xml