Skip to main content
ARS Home » Research » Publications at this Location » Publication #128194
Title: IDENTIFICATION OF NOVEL POLYPEPTIDES IN A HIGHLY PURIFIED PHOTOSYSTEM II PREPARATION FROM THE CYANOBACTERIUM SYNECHOCYSTIS SP. PCC 6803

Author
item KASHINO, K - WASHINGTON U ST. LOUIS MO
item LAUBER, WENDY - PHARMACIA CO ST. LOUIS MO
item CARROLL, JAMES - PHARMACIA CO ST. LOUIS MO
item WANG, QINGIUN - BIOPHYSICS UOFI URBANA IL
item WHITMARSH, CLIFFORD
item SATOH, KAZUHIKO - WASHINGTON U ST. LOUIS MO
item PAKRASI, HIMADRI - WASHINGTON U ST. LOUIS MO

Submitted to: International Congress of Photosynthesis Brisbane Australia
Publication Type: Proceedings
Publication Acceptance Date: 8/25/2001
Publication Date: 12/20/2002
Citation: KASHINO, K., LAUBER, W.M., CARROLL, J.A., WANG, Q., WHITMARSH, C.J., SATOH, K., PAKRASI, H.B. Identification of novel polypeptides in a highly purified photosystem II preparation from the ctabibacteruyn synechocystis SP. PCC 6803. International Congress Of Photosynthesis, Brisbane, Australia. 2002. v. 41. p. 8004-3012.

Interpretive Summary:

Technical Abstract: A highly active oxygen-evolving photosystem II complex was purified from the cyanobacterium Synechocystis sp. PCC 6803. Measurements of oxygen evolution and chlorophyll fluorescence kinetics show that the purified complex are intact and active. Protein analysis using a system designed to enhance resolution of low molecular weight polypeptides, followed by MALDI mass spectrometry and N-terminal amino acid sequencing, identified 31 distinct polypeptides in this purified PSII complex. Other novel photosystem II polypeptides include the FtsH protease involved in the degradation of the D1 protein and the sll1638 gene product, which has significant sequence similarity to PsbQ, a peripheral protein of photosystem II in chloroplasts. This work describes newly identified polypeptides in a highly purified cyanobacterial photosystem II preparation that can be used to investigate the structure, function, and biogenesis of this photosystem.