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

FEBS Letters

Vener, Alexander V¹  Edvardsson, Anna¹  Eshaghi, Said¹  Andersson, Bertil¹ 

[1] Division of Cell Biology, Linköping University, SE-581 85 Linköping, Sweden

关键词: Cyclophilin;    Mass spectrometry;    Peptidyl-prolyl isomerase activity;    Spinach;    Thylakoid lumen;    CsA;    cyclosporin A;    FKBP;    FK506 binding protein;    PPIase;    peptidyl-prolyl cis/trans isomerase;    TLP20;    thylakoid lumen PPIase of 20 kDa;    TLP40;    thylakoid lumen PPIase of 40 kDa;   

DOI  :  10.1016/S0014-5793(03)00366-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 (hylakoid umen PIase of 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.

【 授权许可】

Unknown