TOPOLOGY AND SUBCELLULAR-LOCALIZATION OF FTSH PROTEIN IN ESCHERICHIA-COLI

被引:146
作者
TOMOYASU, T
YAMANAKA, K
MURATA, K
SUZAKI, T
BOULOC, P
KATO, A
NIKI, H
HIRAGA, S
OGURA, T
机构
[1] KUMAMOTO UNIV,SCH MED,INST MOLEC EMBRYOL & GENET,DEPT MOLEC,KUMAMOTO 862,JAPAN
[2] HIROSHIMA UNIV,FAC INTEGRATED ARTS & SCI,CELL BIOL LABS,HIROSHIMA 730,JAPAN
[3] NIPPON INST BIOL SCI,OME,TOKYO 198,JAPAN
[4] UNIV PARIS 07,INST JACQUES MONROD,CNRS,F-75251 PARIS 05,FRANCE
关键词
D O I
10.1128/JB.175.5.1352-1357.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
FtsH protein in Escherichia coli is an essential protein of 70.7 kDa (644 amino add residues) with a putative ATP-binding sequence. Western blots (immunoblots) of proteins from fractionated cell extracts and immunoelectron microscopy of the FtsH-overproducing strain showed exclusive localization of the FtsH protein in the cytoplasmic membrane. Most of the FtsH-specific labeling with gold particles was observed in the cytoplasmic membrane and the adjacent cytoplasm; much less was observed in the outer membrane and in the bulk cytoplasm. Genetic analysis by TnphoA insertions into ftsH revealed that the 25- to 95-amino-acid region, which is flanked by two hydrophobic stretches, protrudes into the periplasmic space. From these results, we concluded that FtsH protein is an integral cytoplasmic membrane protein spanning the membrane twice and that it has a large cytoplasmic carboxy-terminal part with a putative ATP-binding domain. The average number of FtsH molecules per cell was estimated to be approximately 400.
引用
收藏
页码:1352 / 1357
页数:6
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