TETRACYCLINE/H+ ANTIPORTER WAS DEGRADED RAPIDLY IN ESCHERICHIA-COLI-CELLS WHEN TRUNCATED AT LAST TRANSMEMBRANE HELIX AND THIS DEGRADATION WAS PROTECTED BY OVERPRODUCED GROEL/ES

被引:12
作者
SATO, K
SATO, MH
YAMAGUCHI, A
YOSHIDA, M
机构
[1] TOKYO INST TECHNOL, RESOURCES UTILIZAT RES LAB, MIDORI KU, YOKOHAMA 227, JAPAN
[2] CHIBA UNIV, FAC PHARMACEUT SCI, DIV MICROBIAL CHEM, CHIBA 260, JAPAN
关键词
D O I
10.1006/bbrc.1994.1921
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 in vivo degradation of the plasmid-encoded tetracycline/H+ antiporter(TET) in Escherichia coli cells was studied using three mutants with carboxyl-terminal truncation at the positions in the hydrophilic carboxyl-terminal tail (TET388), in the last putative transmembrane helix XII (TET382), and immediately before the helix XII (TET365). All the mutant TET proteins were localized in the membrane. Expressed TET388 was active in transport and stable against proteolysis. However, TET382 and TET365 were inactive and proteolyzed rapidly. Thus, the importance of the helix XII for protease-resistant proper folding of TET is obvious. Interestingly, overproduced chaperonin (GroEL and GroES) partly prevented degradation of TET365. (C) 1994 Academic Press, Inc.
引用
收藏
页码:258 / 264
页数:7
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