QQ客服 官方微博 反馈留言

	The new flagella-associated collagen-like proteins ClpB and ClpC of Bacillus amyloliquefaciens FZB42 are involved in bacterial motility
	Zhao, Xia1,2,3; Wang, Ruoyu1,3; Shang, Qianhan1,2,3; Hao, Haiting1,2,3; Li, Yuyao5; Zhang, Yubao1,3; Guo, Zhihong1,3; Wang, Yun4; Xie, Zhongkui1,3
刊名	MICROBIOLOGICAL RESEARCH
	2016
卷号	184页码:25-31
关键词	Collagen-like proteins Immunogold-labeling Flagella Bacteria motility Plant growth promoting rhizobacteria
ISSN号	0944-5013
DOI	10.1016/j.micres.2015.12.004
通讯作者	Wang, Ruoyu(wangruoyu@lzb.ac.cn)
英文摘要	Collagen-like proteins (CLPs) share the distinctive Gly-X-Thr repeating amino acid sequence of animal collagens, and contain N- and C-terminal domain making a collagen-like structure in Bacillus amyloliquefaciens FZB42, a plant growth-promoting rhizobacterium. Our previous study demonstrated that CLPs play important roles in biofilm construction and adherence to the surfaces on plant roots. However, bacterial localization of the CLPs remains unclear. Here, disrupted strains on all four clp genes (clpA, clpB, clpC and clpD) shown fewer filament than wild-type bacteria in extracellular matrix under scanning electron microscope (SEM). Transmission electron microscopy (TEM) was used to observe the differences on filament which associated on the cell surface, then the CLPs mutation strains showed less flagella than the wild type. Immunogold labeling determined the location that ClpB and ClpC localized on the flagella surface. In addition, western blotting analysis of crude flagella extracts suggested that the ClpB and ClpC are associated to flagella as well. The mutation strains also reduced motility of swimming on the surface of soft agar medium and changed the architectural of microcolony biofilm edge. The study suggests that collagen-like protein ClpB and ClpC, as novel proteins, associated with flagella in B. amyloliquefaciens. (C) 2015 Elsevier GmbH. All rights reserved.
收录类别	SCI
WOS关键词	COMPLETE GENOME SEQUENCE ; ICE-NUCLEATION PROTEIN ; GROUP-A STREPTOCOCCUS ; PSEUDOMONAS-AERUGINOSA ; TWITCHING MOTILITY ; BIOFILM FORMATION ; ESCHERICHIA-COLI ; FUNCTIONAL-CHARACTERIZATION ; ANTHRACIS EXOSPORIUM ; SPORE SURFACE
WOS研究方向	Microbiology
WOS类目	Microbiology
语种	英语
出版者	ELSEVIER GMBH, URBAN & FISCHER VERLAG
WOS记录号	WOS:000370903700003
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2557412
专题	寒区旱区环境与工程研究所
通讯作者	Wang, Ruoyu
作者单位	1.Chinese Acad Sci, Cold & Arid Reg Environm & Engn Res Inst, Gaolan Stn Agr & Ecol Expt, Lanzhou, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Key Lab Stress Physiol & Ecol Cold & Arid Reg Gan, Lanzhou, Peoples R China 4.Chinese Acad Sci, Cold & Arid Reg Environm & Engn Res Inst, Key Lab Desert & Desertificat, Lanzhou, Peoples R China 5.Lanzhou Univ, Sch Life Sci, Key Lab Arid & Grassland Agroecol, Lanzhou 730000, Peoples R China
推荐引用方式 GB/T 7714	Zhao, Xia,Wang, Ruoyu,Shang, Qianhan,et al. The new flagella-associated collagen-like proteins ClpB and ClpC of Bacillus amyloliquefaciens FZB42 are involved in bacterial motility[J]. MICROBIOLOGICAL RESEARCH,2016,184:25-31.
APA	Zhao, Xia.,Wang, Ruoyu.,Shang, Qianhan.,Hao, Haiting.,Li, Yuyao.,...&Xie, Zhongkui.(2016).The new flagella-associated collagen-like proteins ClpB and ClpC of Bacillus amyloliquefaciens FZB42 are involved in bacterial motility.MICROBIOLOGICAL RESEARCH,184,25-31.
MLA	Zhao, Xia,et al."The new flagella-associated collagen-like proteins ClpB and ClpC of Bacillus amyloliquefaciens FZB42 are involved in bacterial motility".MICROBIOLOGICAL RESEARCH 184(2016):25-31.

个性服务

查看访问统计

相关权益政策

暂无数据

收藏/分享

除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。