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A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor

Shiyu Wu Orcid Logo, Xue Yu Orcid Logo, Yujie Wu Orcid Logo, Xiaomin Niu, Ximing Chen, Tuo Chen, Wei Zhang, Guangxiu Liu, Paul Dyson Orcid Logo

Microorganisms, Volume: 14, Issue: 4, Start page: 733

Swansea University Author: Paul Dyson Orcid Logo

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DOI (Published version): 10.3390/microorganisms14040733

Abstract

Acyl-CoA carboxylase (YCC) complexes generate essential starter and extender units for fatty acid and polyketide biosynthesis in Actinobacteria. In Streptomyces coelicolor, two tri-subunit YCC complexes, acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC), have been characterized. Howev...

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Published in: Microorganisms
ISSN: 2076-2607
Published: MDPI AG 2026
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URI: https://cronfa.swan.ac.uk/Record/cronfa71717
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spelling 2026-05-07T14:43:49.5990867 v2 71717 2026-04-07 A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor 300e3f46b70ae83f563b24f41d00cd17 0000-0002-0558-2666 Paul Dyson Paul Dyson true false 2026-04-07 MEDS Acyl-CoA carboxylase (YCC) complexes generate essential starter and extender units for fatty acid and polyketide biosynthesis in Actinobacteria. In Streptomyces coelicolor, two tri-subunit YCC complexes, acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC), have been characterized. However, comparative genomic analyses indicate that β/ε subunits are more diversified than currently appreciated. Here, we identify a previously unrecognized β/ε pair, AccB2 and AccE2, and demonstrate that they assemble with the canonical α subunit to form a functional YCC complex. Both genes are transcribed in vivo, and co-immunoprecipitation (Co-IP) reveals association with AccA1 and AccA2, with AccE2 showing stronger relative association with AccA1-containing pull-downs. In vitro reconstitution confirms carboxylation activity toward acetyl-CoA, propionyl-CoA, and butyryl-CoA, which is strongly dependent on AccE2. These findings expand the YCC repertoire in S. coelicolor and support a modular assembly model in which alternative β/ε combinations contribute to functional diversification of YCC complexes. Journal Article Microorganisms 14 4 733 MDPI AG 2076-2607 acyl-CoA carboxylase; Streptomyces coelicolor; tri-subunit complex; β/ε subunits 25 3 2026 2026-03-25 10.3390/microorganisms14040733 COLLEGE NANME Medical School COLLEGE CODE MEDS Swansea University Another institution paid the OA fee This work was financially supported by the Scientific Project of Gansu Province (22ZD6WA035) and the National Natural Science Foundation of China (U22A20451). 2026-05-07T14:43:49.5990867 2026-04-07T16:18:38.2390630 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Biomedical Science Shiyu Wu 0009-0002-8048-4043 1 Xue Yu 0000-0002-1241-4281 2 Yujie Wu 0000-0002-4308-0333 3 Xiaomin Niu 4 Ximing Chen 5 Tuo Chen 6 Wei Zhang 7 Guangxiu Liu 8 Paul Dyson 0000-0002-0558-2666 9 71717__36676__e2b65a77151b4aae98906b9acb1a517f.pdf 71717.VOR.pdf 2026-05-07T14:38:14.2985627 Output 977345 application/pdf Version of Record true © 2026 by the authors. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license. true eng
title A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
spellingShingle A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
Paul Dyson
title_short A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
title_full A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
title_fullStr A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
title_full_unstemmed A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
title_sort A Novel β/ε Subunit Combination Expands the Tri-Subunit Acyl-CoA Carboxylase Repertoire in Streptomyces coelicolor
author_id_str_mv 300e3f46b70ae83f563b24f41d00cd17
author_id_fullname_str_mv 300e3f46b70ae83f563b24f41d00cd17_***_Paul Dyson
author Paul Dyson
author2 Shiyu Wu
Xue Yu
Yujie Wu
Xiaomin Niu
Ximing Chen
Tuo Chen
Wei Zhang
Guangxiu Liu
Paul Dyson
format Journal article
container_title Microorganisms
container_volume 14
container_issue 4
container_start_page 733
publishDate 2026
institution Swansea University
issn 2076-2607
doi_str_mv 10.3390/microorganisms14040733
publisher MDPI AG
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 1
active_str 0
description Acyl-CoA carboxylase (YCC) complexes generate essential starter and extender units for fatty acid and polyketide biosynthesis in Actinobacteria. In Streptomyces coelicolor, two tri-subunit YCC complexes, acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC), have been characterized. However, comparative genomic analyses indicate that β/ε subunits are more diversified than currently appreciated. Here, we identify a previously unrecognized β/ε pair, AccB2 and AccE2, and demonstrate that they assemble with the canonical α subunit to form a functional YCC complex. Both genes are transcribed in vivo, and co-immunoprecipitation (Co-IP) reveals association with AccA1 and AccA2, with AccE2 showing stronger relative association with AccA1-containing pull-downs. In vitro reconstitution confirms carboxylation activity toward acetyl-CoA, propionyl-CoA, and butyryl-CoA, which is strongly dependent on AccE2. These findings expand the YCC repertoire in S. coelicolor and support a modular assembly model in which alternative β/ε combinations contribute to functional diversification of YCC complexes.
published_date 2026-03-25T06:12:52Z
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