Protein phosphorylation in the photosynthetic bacterium Rhodospirillum rubrum

FEBS Letters

Vallejos, Rubén H.¹  Lucero, Héctor A.¹  Holuigue, Loreto¹ 

[1] Centro de Estudios Fotosintéticos y Bioquímicos, Suipacha 531, 2000-Rosario, Argentina (Conicet, F.M. Lillo, Universidad National de Rosario)

关键词: Protein phosphorylation;    Protein kinase;    Photosynthetic bacterium;    Rhodospirillum rubrum;   

DOI  :  10.1016/0014-5793(85)81122-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Endogenous protein phosphorylation in cellular fractions from Rhodospirillum rubrum was manifested after exposure to [γ-³²P]ATP. At least six phosphorylated protein bands of 90, 86, 64, 31, 13 and 11 kDa were found in the cell-free extract. Treatment of the 64-kDa band with V₈ protease yielded smaller radioactive bands. Phosphoserine, phosphothreonine and phosphotyrosine were detected after acid hydrolysis of the phosphorylated fractions. Protein phosphorylation in all the fractions was insensitive to cAMP, did not recognize exogenous protein substrates and was rapidly reverted upon elimination of the excess of [γ-³²P]ATP. The chlorophyll-anthena apoprotein from R. rubrum chromatophores overlapped the 13-kDa phosphorylated band during gel filtration by high-pressure liquid chromatography suggesting that it is one of the substrates of the protein kinase(s) of R. rubrum.

【 授权许可】

Unknown