2009年8月
The peptidoglycan-binding (PGB) Domain of the Escherichia coli Pal Protein can also Function as the PGB Domain in E. coli Flagellar Motor Protein MotB
Journal of Biochemistry
- ,
- ,
- ,
- ,
- 巻
- 146
- 号
- 2
- 開始ページ
- 219
- 終了ページ
- 229
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1093/jb/mvp061
- 出版者・発行元
- OXFORD UNIV PRESS
The bacterial flagellar stator proteins, MotA and MotB, form a complex and are thought to be anchored to the peptidoglycan by the C-terminal conserved peptidoglycan-binding (PGB) motif of MotB. To clarify the role of the C-terminal region, we performed systematic cysteine mutagenesis and constructed a chimeric MotB protein which was replaced with the peptidoglycan-associated lipoprotein Pal. Although this chimera could not restore motility to a motB strain, we were able to isolate two motile revertants. One was F172V in the Pal region and the other was P159L in the MotB region. Furthermore, we attempted to map the MotB Cys mutations in the crystal structure of Escherichia coli Pal. We found that the MotB mutations that affected motility nearly overlapped with the predicted PG-binding residues of Pal. Our results indicate that, although the functions of MotB and Pal are very different, the PGB region of Pal is interchangeable with the PGB region of MotB.
- リンク情報
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- DOI
- https://doi.org/10.1093/jb/mvp061
- CiNii Articles
- http://ci.nii.ac.jp/naid/10026302760
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/19364805
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000268812700009&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1093/jb/mvp061
- ISSN : 0021-924X
- CiNii Articles ID : 10026302760
- PubMed ID : 19364805
- Web of Science ID : WOS:000268812700009