The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20
2003 (English)In: FEBS Letters, ISSN 0014-5793, Vol. 542, no 1-3, 137-141 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2003. Vol. 542, no 1-3, 137-141 p.
Cyclophilin, Mass spectrometry, Peptidyl-prolyl isomerase activity, Spinach, Thylakoid lumen
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-14355DOI: 10.1016/S0014-5793(03)00366-1OAI: oai:DiVA.org:liu-14355DiVA: diva2:23306