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The Bacterial Flagellar Cap as the Rotary Promoter of Flagellin Self-Assembly
Koji Yonekura,1*Saori Maki,1*David Gene Morgan,2David J. DeRosier,3Ferenc Vonderviszt,4Katsumi Imada,1Keiichi Namba15
The growth of the bacterial flagellar filament occurs at
its distal end by self-assembly of flagellin transported from thecytoplasm through the narrow central channel. The cap at the growingend is essential for its growth, remaining stably attached whilepermitting the flagellin insertion. In order to understand theassembly
mechanism, we used electron microscopy to study the structuresof the
cap-filament complex and isolated cap dimer. Five leg-likeanchor
domains of the pentameric cap flexibly adjusted their conformationsto
keep just one flagellin binding site open, indicating a caprotation
mechanism to promote the flagellin self-assembly. Thisrepresents one
of the most dynamic movements in protein structures.
1 Protonic NanoMachine Project, ERATO, JST, 3-4 Hikaridai, Seika, Kyoto 619-0237, Japan.
2 Department of Biophysics, Boston University School
of Medicine, Boston, MA 02118, and Department of Cell Biology, Harvard
Medical School, Boston, MA 02254, USA.
3 Rosenstiel
Basic Medical Sciences Research Center, Brandeis University, Waltham,
MA 02254, USA.
4 Department of Physics, University
of Veszprém, Egyetem Street 10, H-8201 Veszprém, Hungary.
5 Advanced Technology Research Laboratories,
Matsushita Electric Industrial Co., Ltd., 3-4 Hikaridai, Seika, Kyoto
619-0237 Japan.
*
These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail:
keiichi{at}crl.mei.co.jp
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