Skip Navigation


Journal of Biochemistry Advance Access originally published online on April 13, 2009
Journal of Biochemistry 2009 146(2):219-229; doi:10.1093/jb/mvp061
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
146/2/219    most recent
mvp061v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Hizukuri, Y.
Right arrow Articles by Homma, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hizukuri, Y.
Right arrow Articles by Homma, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

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

Yohei Hizukuri, John Frederick Morton, Toshiharu Yakushi*, Seiji Kojima and Michio Homma{dagger}

Division of Biological Science, Graduate School of Science, Nagoya University, Furo-Cho, Chikusa-Ku, Nagoya 464-8602, Japan

{dagger}To whom correspondence should be addressed. Tel: +81-52-789-2991, Fax: +81-52-789-3001, E-mail: g44416a{at}cc.nagoya-u.ac.jp

Received December 22, 2008; Accepted March 25, 2009


  Abstract

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.

Key Words: bacterial flagella, Escherichia coli, MotB, peptidoglycan-binding protein, Pal

Abbreviations: PG, peptidoglycan; PGB, peptidoglycan-binding; TCA, trichloric acid

*Present address: Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi 753-8515, Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.