The high light-inducible polypeptides in Synechocystis PCC6803. Expression and function in high light.

作者: Qingfang He , Nadia Dolganov , Olle Björkman , Arthur R. Grossman

DOI: 10.1074/JBC.M008686200

关键词:

摘要: There are five Synechocystis PCC6803 genes encoding polypeptides with similarity to the Lhc of plants. Four polypeptides, designated HliA-D (Dolganov, N. A. M., Bhaya, D., and Grossman, R. (1995) Proc. Natl. Acad. Sci. U. S. 92, 636-640) (corresponding ScpC, ScpD, ScpB, ScpE in Funk, C., Vermaas, W. (1999) Biochemistry 38, 9397-9404) contain a single transmembrane domain. The fifth polypeptide (HemH) represents fusion between ferrochelatase an Hli-like polypeptide. By using epitope tag identify specifically different Hli accumulation each (excluding HemH) was examined under various environmental conditions. levels all were elevated high light during nitrogen limitation, whereas HliA, HliB, HliC also accumulated following exposure sulfur deprivation low temperature. temporal pattern significantly among polypeptides. rapidly light, its level remained for at least 24 h. HliA HliB rapidly, but their began decline 9-12 h imposition light. HliD transiently expressed not detected after initiation exposure. These results demonstrate that there is specificity diverse range Furthermore, mutants individual combinations hli evaluated fitness grow Although grew as fast wild-type cells strains inactivated hliA or hliC/hliD unable compete co-cultivation A mutant lacking four gradually lost photosynthesis capacity died Hence, critical survival when absorbing excess excitation energy may allow cope more effectively production reactive oxygen species.

参考文章(78)
Shih-Ying Hwang, Hui-Wen Lin, Ruey-Houng Chern, Hsiao Feng Lo, Liang Li, Reduced susceptibility to waterlogging together with high-light stress is related to increases in superoxide dismutase and catalase activities in sweet potato Plant Growth Regulation. ,vol. 27, pp. 167- 172 ,(1999) , 10.1023/A:1006100508910
I Adamska, K Kloppstech, I Ohad, UV light stress induces the synthesis of the early light-inducible protein and prevents its degradation. Journal of Biological Chemistry. ,vol. 267, pp. 24732- 24737 ,(1992) , 10.1016/S0021-9258(18)35825-3
I. Adamska, K. Kloppstech, I. Ohad, Early light-inducible protein in pea is stable during light stress but is degraded during recovery at low light intensity. Journal of Biological Chemistry. ,vol. 268, pp. 5438- 5444 ,(1993) , 10.1016/S0021-9258(18)53340-8
Stefan Jansson, Jenny Andersson, Soo Jung Kim, Grzegorz Jackowski, An Arabidopsis thaliana protein homologous to cyanobacterial high-light-inducible proteins Plant Molecular Biology. ,vol. 42, pp. 345- 351 ,(2000) , 10.1023/A:1006365213954
E. M. Aro, S. McCaffery, J. M. Anderson, Photoinhibition and D1 Protein Degradation in Peas Acclimated to Different Growth Irradiances Plant Physiology. ,vol. 103, pp. 835- 843 ,(1993) , 10.1104/PP.103.3.835
G.F. Peter, J.P. Thornber, Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins. Journal of Biological Chemistry. ,vol. 266, pp. 16745- 16754 ,(1991) , 10.1016/S0021-9258(18)55364-3