The N-terminal sequence after residue 247 plays an important role in structure and function of Lon protease from Brevibacillus thermoruber WR-249

被引：11

作者：

Chir, Jiun-Ly ^{[1
]}

Liao, Jiahn-Haur ^{[1
]}

Lin, Yu-Ching ^{[2
]}

Wu, Shih-Hsiung ^{[1
,2
]}

机构：

[1] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan

[2] Natl Taiwan Univ, Inst Biochem Sci, Taipei 106, Taiwan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 382卷 / 04期

关键词：

Lon protease; ATP-dependent protease; Gel filtration chromatography; Brevibacillus thermoruber; ESCHERICHIA-COLI LON; LIMITED PROTEOLYSIS; LA LON; DOMAIN; SUBSTRATE; BINDING; ENZYME; SITE; CLASSIFICATION; DNA;

D O I：

10.1016/j.bbrc.2009.03.109

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Previous studies on the N-terminal domain of Lon proteases have not clearly identified its function. Here we constructed randomly chosen N-terminal-truncated mutants of the Lon protease from Brevibacillus thermoruber WR-249 to elucidate tire structure-function relationship of this domain. Mutants lacking amino acids from 1 to 247 of N terminus retained significant peptidase and ATPase activities, but lost similar to 90% of protease activity. Further truncation of the protein resulted in the loss of all three activities. Mutants lacking amino acids 246-259 or 248-256 also lost all activities and quaternary structure. Our results indicated that amino acids 248-256 (SEVDELRAQ) are important for the full function of the Lon protease. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：762 / 765

页数：4

共 20 条

[1]

SITE-DIRECTED MUTAGENESIS OF LA PROTEASE - A CATALYTICALLY ACTIVE SERINE RESIDUE [J].