Proteome Map of the Chloroplast Lumen of Arabidopsis thaliana

• Published in: The Journal of biological chemistry 2002-03, Vol.277 (10), p.8354-8365
• Main Authors: Schubert, Maria, Petersson, Ulrika A., Haas, Brian J., Funk, Christiane, Schröder, Wolfgang P., Kieselbach, Thomas
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Arabidopsis - chemistry; Arabidopsis - physiology; Cell Division; Chloroplasts - chemistry; Electrophoresis, Gel, Two-Dimensional; Genome, Plant; Molecular Sequence Data; Plant Physiological Phenomena; Protein Binding; Protein Structure, Tertiary; Silver Staining; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spinacia oleracea; Thylakoids - chemistry
• ISSN: 0021-9258; 1083-351X; 1083-351X
• DOI: 10.1074/jbc.M108575200

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 proteases, 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 organismArabidopsis 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 Arabidopsisgenome and estimated that the thylakoid lumen of the chloroplast contains ∼80 proteins.