Journal article 90 views
A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
Matthew Aldridge,
Paul Facey 
,
Lewis Francis,
Sion Bayliss,
Ricardo Del Sol,
Paul Dyson
,
Lewis Francis,
Sion Bayliss,
Ricardo Del Sol,
Paul Dyson
Nucleic Acids Research, Volume: 41, Issue: 9, Pages: 4813 - 4824
Swansea University Author:
Paul Facey
Full text not available from this repository: check for access using links below.
DOI (Published version): 10.1093/nar/gkt180
Abstract
Antibiotic-producing Streptomyces are complex bacteria that remodel global transcription patterns and their nucleoids during development. Here, we describe a novel developmentally regulated nucleoid-associated protein, DdbA, of the genus that consists of an N-terminal DNA-binding histone H1-like dom...
| Published in: | Nucleic Acids Research |
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| ISSN: | 0305-1048 1362-4962 |
| Published: |
Oxford University Press (OUP)
2013
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| Online Access: |
Check full text
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| URI: | https://cronfa.swan.ac.uk/Record/cronfa70402 |
| Abstract: |
Antibiotic-producing Streptomyces are complex bacteria that remodel global transcription patterns and their nucleoids during development. Here, we describe a novel developmentally regulated nucleoid-associated protein, DdbA, of the genus that consists of an N-terminal DNA-binding histone H1-like domain and a C-terminal DksA-like domain that can potentially modulate RNA polymerase activity in conjunction with ppGpp. Owing to its N-terminal domain, the protein can efficiently bind and condense DNA in vitro . Loss of function of this DNA-binding protein results in changes in both DNA condensation during development and the ability to adjust DNA supercoiling in response to osmotic stress. Initial analysis of the DksA-like activity of DdbA indicates that overexpression of the protein suppresses a conditional deficiency in antibiotic production of relA mutants that are unable to synthesise ppGpp, just as DksA overexpression in Escherichia coli can suppress ppGpp 0 phenotypes. The null mutant is also sensitive to oxidative stress owing to impaired upregulation of transcription of sigR , encoding an alternative sigma factor. Consequently, we propose this bifunctional histone-like protein as a candidate that could structurally couple changes in DNA conformation and transcription during the streptomycete life-cycle and in response to stress. |
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| College: |
Faculty of Medicine, Health and Life Sciences |
| Funders: |
European Commission [FP6, LSH-IP 005224, ActinoGen]; European Social Fund grant (to M.A.). |
| Issue: |
9 |
| Start Page: |
4813 |
| End Page: |
4824 |