Expression, purification and preliminary crystallization study of RpaC protein from Synechocystis sp PCC6803

0341135 - ÚVGZ 2013 RIV NL eng J - Journal Article
Cséfalvay, Eva - Lapkouski, Mikalai - Komárek, Ondřej
Expression, purification and preliminary crystallization study of RpaC protein from Synechocystis sp PCC6803.
Photosynthetica. Roč. 3, č. 47 (2009), s. 355-362. ISSN 0300-3604. E-ISSN 1573-9058
R&D Projects: GA ČR GA206/07/0917
Institutional research plan: CEZ:AV0Z60870520
Keywords : affinity chromatography * photosystem * phycobilisome – PSII supercomplex
Subject RIV: CE - Biochemistry
Impact factor: 1.072, year: 2009

State transitions in cyanobacteria are physiological adaptation mechanisms that change the interaction of the phycobilisomes with the photosystem I and photosystem II core complexes. Previous studies of cyanobacteria have identified a gene named rpaC, which appears to be specifically required for state transitions. The gene product of rpaC is very probably a transmembrane protein that is a structural component of the phycobilisome-photosystem II supercomplex. Here we report the construction of an expression system that enables high production of fusion protein TrxHisTagSTag-RpaC, and describe suitable conditions for purification of this insoluble protein at a yield of 3 mg per 1 dm3 of bacterial culture.
Permanent Link: http://hdl.handle.net/11104/0184214