气候变化领域集成服务门户(CCPortal): Evolution of a σ–(c-di-GMP)

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DOI	10.1073/pnas.2105447118
	Evolution of a σ–(c-di-GMP)–anti-σ switch
	Schumacher M.A.; Gallagher K.A.; Holmes N.A.; Chandra G.; Henderson M.; Kysela D.T.; Brennan R.G.; Buttner M.J.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:30
英文摘要	Filamentous actinobacteria of the genus Streptomyces have a complex lifecycle involving the differentiation of reproductive aerial hyphae into spores. We recently showed c-di-GMP controls this transition by arming a unique anti-σ, RsiG, to bind the sporulation-specific σ, WhiG. The Streptomyces venezuelae RsiG–(c-di-GMP)2–WhiG structure revealed that a monomeric RsiG binds c-di-GMP via two E(X)3S(X)2R(X)3Q(X)3D repeat motifs, one on each helix of an antiparallel coiled-coil. Here we show that RsiG homologs are found scattered throughout the Actinobacteria. Strikingly, RsiGs from unicellular bacteria descending from the most basal branch of the Actinobacteria are small proteins containing only one c-di-GMP binding motif, yet still bind their WhiG partners. Our structure of a Rubrobacter radiotolerans (RsiG)2–(c-di-GMP)2–WhiG complex revealed that these single-motif RsiGs are able to form an antiparallel coiled-coil through homodimerization, thereby allowing them to bind c-di-GMP similar to the monomeric twin-motif RsiGs. Further data show that in the unicellular actinobacterium R. radiotolerans, the (RsiG)2–(c-di-GMP)2–WhiG regulatory switch controls type IV pilus expression. Phylogenetic analysis indicates the single-motif RsiGs likely represent the ancestral state and an internal gene-duplication event gave rise to the twin-motif RsiGs inherited elsewhere in the Actinobacteria. Thus, these studies show how the anti-σ RsiG has evolved through an intragenic duplication event from a small protein carrying a single c-di-GMP binding motif, which functions as a homodimer, to a larger protein carrying two c-di-GMP binding motifs, which functions as a monomer. Consistent with this, our structures reveal potential selective advantages of the monomeric twin-motif anti-σ factors. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	C-di-GMP signaling; Protein evolution; RsiG; Second messenger; Streptomyces
语种	英语
scopus关键词	bacterial protein; guanosine phosphate; homodimer; protein RsiG; unclassified drug; bis(3',5')-cyclic diguanylic acid; cyclic GMP; protein binding; sigma factor; Actinobacteria; ancestry group; Article; bacterium pilus; controlled study; gene duplication; homodimerization; molecular evolution; nonhuman; phylogeny; protein binding; protein function; protein motif; protein structure; sporogenesis; Streptomyces venezuelae; structure analysis; fimbria; gene expression regulation; genetics; metabolism; molecular model; protein conformation; protein domain; Streptomyces; X ray crystallography; Actinobacteria; Crystallography, X-Ray; Cyclic GMP; Fimbriae, Bacterial; Gene Expression Regulation, Bacterial; Models, Molecular; Protein Binding; Protein Conformation; Protein Domains; Sigma Factor; Streptomyces
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/251107
作者单位	Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, United States; Department of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, United Kingdom; Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montreal, QC H3T 1J4, Canada
推荐引用方式 GB/T 7714	Schumacher M.A.,Gallagher K.A.,Holmes N.A.,等. Evolution of a σ–(c-di-GMP)–anti-σ switch[J],2021,118(30).
APA	Schumacher M.A..,Gallagher K.A..,Holmes N.A..,Chandra G..,Henderson M..,...&Buttner M.J..(2021).Evolution of a σ–(c-di-GMP)–anti-σ switch.Proceedings of the National Academy of Sciences of the United States of America,118(30).
MLA	Schumacher M.A.,et al."Evolution of a σ–(c-di-GMP)–anti-σ switch".Proceedings of the National Academy of Sciences of the United States of America 118.30(2021).