Lysine acetylation regulates the function of the global anaerobic transcription factor FnrL in Rhodobacter sphaeroides. Issue 2 (28th February 2017)
- Record Type:
- Journal Article
- Title:
- Lysine acetylation regulates the function of the global anaerobic transcription factor FnrL in Rhodobacter sphaeroides. Issue 2 (28th February 2017)
- Main Title:
- Lysine acetylation regulates the function of the global anaerobic transcription factor FnrL in Rhodobacter sphaeroides
- Authors:
- Wei, Wei
Liu, Tong
Li, Xinfeng
Wang, Ruofan
Zhao, Wei
Zhao, Guoping
Zhao, Shimin
Zhou, Zhihua - Abstract:
- Summary: The metabolism of the purple non‐sulfur bacterium Rhodobacter sphaeroides is versatile and it can grow under various conditions. Here, we report evidence that the anaerobic photosynthetic metabolism of R. sphaeroides is regulated by protein lysine acetylation. Using a proteomic approach, 59 acetylated peptides were detected. Among them is the global anaerobic transcription factor FnrL, which regulates the biosynthetic pathway of tetrapyrroles and synthesis of the photosynthetic apparatus. Lysine 223 of FnrL was identified as acetylated. We show that all three lysines in the DNA binding domain (K223, K213 and K175) of FnrL can be acetylated by acetyl‐phosphate in vitro . A bacterial deacetylase homolog, RsCobB can deacetylate FnrL in vitro . The transcription of genes downstream of FnrL decreased when the DNA binding domain of FnrL was acetylated, as revealed by chromatin immunoprecipitation and acetylation‐mimicking mutagenesis. An increasing number of acetylated lysines resulted in a further decrease in DNA binding ability. These results demonstrate that the lysine acetylation can fine tune the function of the oxygen‐sensitive FnrL; thus, it might regulate anaerobic photosynthetic metabolism of R. sphaeroides . Abstract : Acetyl‐phosphate and bacterial deacetylase homolog RsCobB can reverse the acetylation of the global anaerobic transcription factor FnrL of Rhodobacter sphaeroides . Acetylated FnrL decreases the DNA binding capability with the promoters of itsSummary: The metabolism of the purple non‐sulfur bacterium Rhodobacter sphaeroides is versatile and it can grow under various conditions. Here, we report evidence that the anaerobic photosynthetic metabolism of R. sphaeroides is regulated by protein lysine acetylation. Using a proteomic approach, 59 acetylated peptides were detected. Among them is the global anaerobic transcription factor FnrL, which regulates the biosynthetic pathway of tetrapyrroles and synthesis of the photosynthetic apparatus. Lysine 223 of FnrL was identified as acetylated. We show that all three lysines in the DNA binding domain (K223, K213 and K175) of FnrL can be acetylated by acetyl‐phosphate in vitro . A bacterial deacetylase homolog, RsCobB can deacetylate FnrL in vitro . The transcription of genes downstream of FnrL decreased when the DNA binding domain of FnrL was acetylated, as revealed by chromatin immunoprecipitation and acetylation‐mimicking mutagenesis. An increasing number of acetylated lysines resulted in a further decrease in DNA binding ability. These results demonstrate that the lysine acetylation can fine tune the function of the oxygen‐sensitive FnrL; thus, it might regulate anaerobic photosynthetic metabolism of R. sphaeroides . Abstract : Acetyl‐phosphate and bacterial deacetylase homolog RsCobB can reverse the acetylation of the global anaerobic transcription factor FnrL of Rhodobacter sphaeroides . Acetylated FnrL decreases the DNA binding capability with the promoters of its downstream genes, thus weakening their transcription. The increasing number of acetylated lysines can fine tune the DNA binding function of FnrL, regulating the anaerobic photosynthetic metabolism. … (more)
- Is Part Of:
- Molecular microbiology. Volume 104:Issue 2(2017)
- Journal:
- Molecular microbiology
- Issue:
- Volume 104:Issue 2(2017)
- Issue Display:
- Volume 104, Issue 2 (2017)
- Year:
- 2017
- Volume:
- 104
- Issue:
- 2
- Issue Sort Value:
- 2017-0104-0002-0000
- Page Start:
- 278
- Page End:
- 293
- Publication Date:
- 2017-02-28
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13627 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2602.xml