The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

被引：36

作者：

Edvardsson, A

Eshaghi, S

Vener, AV ^{[1
]}

Andersson, B

机构：

[1] Linkoping Univ, Div Cell Biol, SE-58185 Linkoping, Sweden

[2] Stockholm Univ, Arrhenius Labs Nat Sci, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden

来源：

FEBS LETTERS | 2003年 / 542卷 / 1-3期

基金：

瑞典研究理事会;

关键词：

cyclophilin; mass spectrometry; peptidyl-prolyl isomerase activity; spinach; thylakoid lumen;

D O I：

10.1016/S0014-5793(03)00366-1

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：

Fractionation of proteins from the thylakoid lumen of spinach chloroplasts combined with peptidyl-prolyl cis/trans isomerase (PPIase) measurements revealed a major isomerase activity that was ascribed to a novel enzyme TLP20 (thylakoid lumen PPIase of 20 kDa). TLP20 was inhibited by cyclosporin A and mass spectrometric sequencing of tryptic peptides confirmed its classification as a cyclophilin. Genes encoding similar putative thylakoid cyclophilins with a unique insert of three amino acids NPV in their N-termini were found in chromosome 5 of both Arabidopsis and rice. TLP20 is suggested to be the major PPIase and protein folding catalyst in the thylakoid lumen of plant chloroplasts. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：137 / 141

页数：5

共 25 条

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