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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 Orcid Logo, Lewis Francis, Sion Bayliss, Ricardo Del Sol, Paul Dyson

Nucleic Acids Research, Volume: 41, Issue: 9, Pages: 4813 - 4824

Swansea University Author: Paul Facey Orcid Logo

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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...

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Published in: Nucleic Acids Research
ISSN: 0305-1048 1362-4962
Published: Oxford University Press (OUP) 2013
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URI: https://cronfa.swan.ac.uk/Record/cronfa70402
first_indexed 2025-09-18T22:01:47Z
last_indexed 2025-11-04T15:02:00Z
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spelling 2025-11-03T09:39:13.8535843 v2 70402 2025-09-18 A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress? dc25910b8004b2694df68ed7426e1286 0000-0002-3229-0255 Paul Facey Paul Facey true false 2025-09-18 MEDS 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. Journal Article Nucleic Acids Research 41 9 4813 4824 Oxford University Press (OUP) 0305-1048 1362-4962 1 5 2013 2013-05-01 10.1093/nar/gkt180 COLLEGE NANME Medical School COLLEGE CODE MEDS Swansea University European Commission [FP6, LSH-IP 005224, ActinoGen]; European Social Fund grant (to M.A.). 2025-11-03T09:39:13.8535843 2025-09-18T20:11:50.8459347 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Biomedical Science Matthew Aldridge 1 Paul Facey 0000-0002-3229-0255 2 Lewis Francis 3 Sion Bayliss 4 Ricardo Del Sol 5 Paul Dyson 6
title A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
spellingShingle A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
Paul Facey
title_short A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
title_full A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
title_fullStr A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
title_full_unstemmed A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
title_sort A novel bifunctional histone protein in Streptomyces : a candidate for structural coupling between DNA conformation and transcription during development and stress?
author_id_str_mv dc25910b8004b2694df68ed7426e1286
author_id_fullname_str_mv dc25910b8004b2694df68ed7426e1286_***_Paul Facey
author Paul Facey
author2 Matthew Aldridge
Paul Facey
Lewis Francis
Sion Bayliss
Ricardo Del Sol
Paul Dyson
format Journal article
container_title Nucleic Acids Research
container_volume 41
container_issue 9
container_start_page 4813
publishDate 2013
institution Swansea University
issn 0305-1048
1362-4962
doi_str_mv 10.1093/nar/gkt180
publisher Oxford University Press (OUP)
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Biomedical Science{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Biomedical Science
document_store_str 0
active_str 0
description 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.
published_date 2013-05-01T05:30:47Z
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score 11.444473

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