Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images
被引:69
作者:
Katayama, E
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机构:TEIKYO UNIV, DEPT BIOSCI, UTSUNOMIYA, TOCHIGI 320, JAPAN
Katayama, E
Shiraishi, T
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机构:TEIKYO UNIV, DEPT BIOSCI, UTSUNOMIYA, TOCHIGI 320, JAPAN
Shiraishi, T
Oosawa, K
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机构:TEIKYO UNIV, DEPT BIOSCI, UTSUNOMIYA, TOCHIGI 320, JAPAN
Oosawa, K
Baba, N
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机构:TEIKYO UNIV, DEPT BIOSCI, UTSUNOMIYA, TOCHIGI 320, JAPAN
Baba, N
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机构:
Aizawa, S
机构:
[1] TEIKYO UNIV, DEPT BIOSCI, UTSUNOMIYA, TOCHIGI 320, JAPAN
[2] KOGAKUIN UNIV, DEPT ELECT ENGN, SHINJUKU KU, TOKYO 160, JAPAN
[3] UNIV TOKYO, INST MED SCI, DEPT FINE MORPHOL, MINATO KU, TOKYO 108, JAPAN
Salmonella typhimurium;
flagellum;
MS ring complex;
quick-freeze deep-etch replica electron microscopy;
digital stereo-photogrammetry;
D O I:
10.1006/jmbi.1996.0038
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The precise geometry of the flagellar basal structure anchored in the cytoplasmic membrane was determined by digital stereo-photogrammetry of the images captured by quick-freeze deep-etch replica electron microscopy. In order to examine the structure on the periplasmic side of the membrane, we analyzed the MS ring complexes of Salmonella typhimurium overproduced in the cytoplasmic membrane of Escherichia coli. The rod, the S ring, and the shoulder of the M ring were exposed to the periplasm. On the cytoplasmic side of the membrane, small bumps corresponding to the cytoplasmic rod were discernible. We also examined the intact inner surface of the cells of polyhook mutant which was prepared by a new protocol and found the bell-shaped structure extending from the membrane towards the cytoplasm. It was identified as the C ring, since it was located at the base of the polyhook. Various dimensions of the MS ring complex and the C ring projecting from the membrane were determined by digital stereo-photogrammetry, and a three-dimensional model of the total basal structure is presented. (C) 1996 Academic Press Limited