Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion

doi:10.3389/fcimb.2018.00080

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	Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion
	Chen, Shiyun 4; Francis, Matthew S.1,3; Gurung, Jyoti M.1,3; Amer, Ayad A. A.1,3; Francis, Monika K.1,3; Costa, Tiago R. D.1,2,3; Zavialov, Anton V.5
刊名	FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY
	2018-03-16
卷号	8 页码:16
关键词	T3S chaperone secretion hierarchy substrate sorting LcrH/SycD YscV protein-protein interaction
ISSN号	2235-2988
DOI	10.3389/fcimb.2018.00080
英文摘要	Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic Yersinia species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an yscX nor yscY null mutant of Yersinia is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of Pseudomonas aeruginosa (PscX and PscY), Aeromonas species (AscX and AscY), Vibrio species (VscX and VscY), and Photorhabdus luminescens (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native yscX in the near full-length yscX deletion and native yscY in the near full-length yscY deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for Yersinia type III secretion.
资助项目	Swedish Research Council[2009-5628] ; Swedish Research Council[2014-2105] ; Foundation for Medical Research at Umea University ; Faculty of Science and Technology at Umea University
WOS研究方向	Immunology ; Microbiology
语种	英语
出版者	FRONTIERS MEDIA SA
WOS记录号	WOS:000427608900001
内容类型	期刊论文
源URL	[http://202.127.146.157/handle/2RYDP1HH/4803]
专题	中国科学院武汉植物园
通讯作者	Francis, Matthew S.
作者单位	1.Umea Univ, Umea Ctr Microbial Res, Umea, Sweden 2.Imperial Coll London, Dept Life Sci, MRC Ctr Mol Bacteriol & Infect, London, England 3.Umea Univ, Dept Mol Biol, Umea, Sweden 4.Chinese Acad Sci, Key Lab Special Pathogens & Biosafety, Wuhan Inst Virol, Wuhan, Hubei, Peoples R China 5.Univ Turku, Dept Chem, Turku, Finland
推荐引用方式 GB/T 7714	Chen, Shiyun,Francis, Matthew S.,Gurung, Jyoti M.,et al. Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion[J]. FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY,2018,8:16.
APA	Chen, Shiyun.,Francis, Matthew S..,Gurung, Jyoti M..,Amer, Ayad A. A..,Francis, Monika K..,...&Zavialov, Anton V..(2018).Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion.FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY,8,16.
MLA	Chen, Shiyun,et al."Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion".FRONTIERS IN CELLULAR AND INFECTION MICROBIOLOGY 8(2018):16.