Importance of a repetitive nine-residue sequence motif for intracellular stability and functional structure of a family I.3 lipase

被引：24

作者：

Angkawidjaja, C

Paul, A

Koga, Y

Takano, K

Kanaya, S

机构：

[1] Osaka Univ, Grad Sch Engn, Dept Mat & Life Sci, Suita, Osaka 5650871, Japan

[2] JST, PRESTO, Suita, Osaka 5650871, Japan

来源：

FEBS LETTERS | 2005年 / 579卷 / 21期

关键词：

family I.3 lipase; type I secretion system; beta-roll; mutation; Ca2+ binding; Pseudomonas;

D O I：

10.1016/j.febslet.2005.07.041

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：

PML5 is a functional derivative of a family I.3 lipase from Pseudomonas sp. MIS38 and contains five repeats of a nine-residue sequence motif. Two aspartate residues within the second and third repetitive sequences of PML5 were replaced by Ala. The secretion level, intracellular accumulation level, and stability of the resultant mutant protein were greatly reduced as compared to those of PML5. In addition, this mutant protein was inactive and did not bind Ca2+ ion. We propose that the repetitive sequences of PML5 form a beta-roll structure in the cells and thereby contribute to the intracellular stability and secretion efficiency of the protein. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：4707 / 4712

页数：6

共 32 条

[1] Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases [J].