气候变化领域集成服务门户(CCPortal): Cooperation of two distinct coupling proteins creates chemosensory network connections

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DOI	10.1073/pnas.1618227114
	Cooperation of two distinct coupling proteins creates chemosensory network connections
	Abedrabbo S.; Castellon J.; Collins K.D.; Johnson K.S.; Ottemann K.M.
发表日期	2017
ISSN	0027-8424
起始页码	2970
结束页码	2975
卷号	114 期号:11
英文摘要	Although it is appreciated that bacterial chemotaxis systems rely on coupling, also called scaffold, proteins to both connect input receptors with output kinases and build interkinase connections that allow signal amplification, it is not yet clear why many systems use more than one coupling protein. We examined the distinct functions for multiple coupling proteins in the bacterial chemotaxis system of Helicobacter pylori, which requires two nonredundant coupling proteins for chemotaxis: CheW and CheV1, a hybrid of a CheW and a phosphorylatable receiver domain. We report that CheV1 and CheW have largely redundant abilities to interact with chemoreceptors and the CheA kinase, and both similarly activated CheA's kinase activity. We discovered, however, that they are not redundant for formation of the higher order chemoreceptor arrays that are known to form via CheA - CheW interactions. In support of this possibility, we found that CheW and CheV1 interact with each other and with CheA independent of the chemoreceptors. Therefore, it seems that some microbes have modified array formation to require CheW and CheV1. Our data suggest that multiple coupling proteins may be used to provide flexibility in the chemoreceptor array formation.
英文关键词	Chemoreceptor arrays; Chemotaxis; Scaffold; Signal transduction
语种	英语
scopus关键词	CheA kinase; protein; bacterial protein; carrier protein; methyl accepting chemotaxis protein; protein binding; autophosphorylation; carboxy terminal sequence; chemoreceptor; chemosensitivity; chemotaxis; complex formation; Conference Paper; Helicobacter pylori; immunofluorescence; phosphorylation; polyacrylamide gel electrophoresis; priority journal; protein localization; protein protein interaction; signal transduction; Western blotting; amino acid sequence; chemistry; metabolism; physiology; signal transduction; Amino Acid Sequence; Bacterial Proteins; Carrier Proteins; Chemotaxis; Methyl-Accepting Chemotaxis Proteins; Phosphorylation; Protein Binding; Signal Transduction
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/160654
作者单位	Abedrabbo, S., Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA 95064, United States; Castellon, J., Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA 95064, United States; Collins, K.D., Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA 95064, United States; Johnson, K.S., Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA 95064, United States; Ottemann, K.M., Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, CA 95064, United States
推荐引用方式 GB/T 7714	Abedrabbo S.,Castellon J.,Collins K.D.,et al. Cooperation of two distinct coupling proteins creates chemosensory network connections[J],2017,114(11).
APA	Abedrabbo S.,Castellon J.,Collins K.D.,Johnson K.S.,&Ottemann K.M..(2017).Cooperation of two distinct coupling proteins creates chemosensory network connections.Proceedings of the National Academy of Sciences of the United States of America,114(11).
MLA	Abedrabbo S.,et al."Cooperation of two distinct coupling proteins creates chemosensory network connections".Proceedings of the National Academy of Sciences of the United States of America 114.11(2017).