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Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986;167(2):233-9doi: 10.1007/BF00391420.
Hei, W. G., & Senger, H. (1986). Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta, 167(2), 233-9. https://doi.org/10.1007/BF00391420
Hei, W G, and Senger, H. "Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture." Planta vol. 167,2 (1986): 233-9. doi: https://doi.org/10.1007/BF00391420
Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420. PMID: 24241856.
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Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420.

Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture.

Planta

W G Hei, H Senger

Affiliations

  1. Fachbereich Biologie-Botanik, Philipps-Universität, Lahnberge, D-3550, Marburg, Federal Republic of Germany.

PMID: 24241856 DOI: 10.1007/BF00391420

Abstract

The phosphorylation of thylakoid proteins, which comprise apoproteins of the light-harvesting chlorophyll a/b-protein complex (LHCP), was investigated in vivo and in vitro during the development of Scenedesmus obliquus in synchronous cultures. The in-vitro and in-vivo protein phosphorylation exhibited a maximum activity in cells with maximum photosynthetic capacity (8th hour) and miximum activity in cells with minimum photosynthetic capacity (16th hour). The major phosphorylated polypeptides in vivo were the 24/25-kDa and 28-30-kDa apoprotein of the LHCP, a protein of about 32 kDa, and some smaller polypeptides within the range 10 to 20 kDa. In vitro, the main phosphoproteins were the 28-30-kDa apoprotein and the protein characterized by an apparent molecular weight of 32 kDa. Pulse-chase experiments in vivo established that the latter had the fastest radioactivity turnover of the thylakoidal phosphoproteins.

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