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Proteome map of the chloroplast lumen of Arabidopsis thaliana
Södertörn University, Avdelning Naturvetenskap. Karolinska Institute.
Södertörn University, Avdelning Naturvetenskap. Stockholm University.
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2002 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, no 10, 8354-8365 p.Article in journal (Refereed) Published
Abstract [en]

The thylakoid membrane of the chloroplast is the center of oxygenic photosynthesis. To better understand the function of the luminal compartment within the thylakoid network, we have carried out a systematic characterization of the luminal thylakoid proteins from the model organism Arabidopsis thaliana. Our data show that the thylakoid lumen has its own specific proteome, of which 36 proteins were identified. Besides a large group of peptidyl-prolyl cis-trans isomerases and pro. teases, a family of novel PsbP domain proteins was found. An analysis of the luminal signal peptides showed that 19 of 36 luminal precursors were marked by a twin-arginine motif for import via the Tat pathway. To compare the model organism Arabidopsis with another typical higher plant, we investigated the proteome from the thylakoid lumen of spinach and found that the luminal proteins from both plants corresponded well. As a complement to our experimental investigation, we made a theoretical prediction of the luminal proteins from the whole Arabidopsis genome and estimated that the thylakoid lumen of the chloroplast contains similar to80 proteins.

Place, publisher, year, edition, pages
2002. Vol. 277, no 10, 8354-8365 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:sh:diva-15812DOI: 10.1074/jbc.M108575200ISI: 000174268000094PubMedID: 11719511ScopusID: 2-s2.0-0037040944OAI: oai:DiVA.org:sh-15812DiVA: diva2:508477
Available from: 2012-03-08 Created: 2012-03-07 Last updated: 2014-04-17Bibliographically approved

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Schubert, MariaPetersson, Ulrika ASchröder, Wolfgang P
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