Characterization of a spinach psbS cDNA encoding the 22 kDa protein of photosystem II

FEBS Letters

Pichersky, Eran¹  Vlahaskis, Sari²  Kim, Sunyoung¹  Sandusky, Peter¹  Yocum, Charles F.¹  Aebersold, Ruedi⁴  Bowlby, Neil R.⁵  Green, Beverley R.³ 

[1] Biology Department, University of Michigan, Ann Arbor, MI 48109, USA;Protein and Carbohydrate Structure Facility, University of Michigan, Ann Arbor, MI 48109, USA;Botany Department, University of British Columbia, Vancouver, BC, V6T 1WS Canada;Biomedical Research Centre and Biochemistry Department, University of British Columbia, Vancouver, BC, V6T 1WS Canada;MSU/DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA

关键词: Pholosystem II;    Polypeptide;    Chlorophyll a/b-binding (CAB) protein;    Gene evolution;   

DOI  :  10.1016/0014-5793(92)81463-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An intrinsic 22 kDa polypeptide is found associated with the oxygen-evolving photesytem II (PSII) core complex in all green plants and cyanobacteria so far examined, although it does not appear to be required for oxygen evolution. Amino acid sequence information obtained from the purified 22 kDa protein was used to construct a probe that was employed to isolate a full-length cDNA clone encoding the 274-residue precursor of the 22 kDa protein. Hydropathy plot analysis predicts the existence of four membrane-spanning helices in the mature protein. The two halves of the approximattely 200-residue mature protein show high sequence similarity to each other, suggesting that the psbS gene arose from an internal gene duplication. The 22 kDa protein has some sequence similarity to chlorophyll a/b-binding, proteins.

【 授权许可】

Unknown