Chlorophyll binding protein

U. Johanningmeier, S. H. Howell (1984) Regulation of light-harvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardtii. Possible involvement of chlorophyll synthesis precursors. J. Biol. Chem., 259 13541-13549... 

Genes down-Rice regulated by low temperature Rubisco ssu Cab Chlorophyll binding protein Hahn Walbot, 1989... 

Morgan TR, Shand JA, Clarke SM et al. Specific requirements for cytochrome c-550 and the manganese- stabilizii protein in photoautotrophic strains of Synechocystis sp. PCC 6803 with mutations in the domain Gly-351 to Thr-436 of the chlorophyll-binding protein CP47 Biochemistry 1998 37 14437-14449. 

Barber J, Morris EP, Buchel C. Revealing the struemre of the photosystem two chlorophyll binding proteins, CP43 and CP47. Biochim Biophys Acta 2000 145 239-247. 

Mori H, Yamashita Y, Akasaka T et al. Further characterization of the loss of antenna chlorophyll-binding protein CP43 from photosystem II during donor-side photoinhibidon. Biochim Biophys Acta 1995 1228 37-42. 

Liu, H., Huang, R.Y.C., Chen, J., et al. (2011) Psb27, A Transiently Associated Protein, Binds to the Chlorophyll Binding Protein CP43 in Photosystem II Assembly Intermediates. Proceedings of the National Academy of Sciences of the United States of America, 108 (45), 18536-18541. 

Fractionation of PSII membranes into discrete subsets. The methods of lEF and immunoblotting give us the possibility to separate and identifie chlorophyll-binding proteins both in native conditions, usefull for the study of protein—protein interactions and fully denaturing conditions indispensable when the quantitative relations between apoproteins must be determined. These... 

Shown in this model are phycobilisome (PBS), reaction center of PSII (RCII), PSn core chlorophyll-binding proteins (CP), and oxygen-evolving complex (OEC). Darkened stmctures indicate components in a nonfunctional form. 

I.the pigment-protein complex PSl of cyanobacteria is a compact closed body composed of 5 low-molecular polypeptides surrounded by two chlorophyll-binding proteins (the pigment antenna system) forming a protective shield which hinders access to small polypeptides from the surface of the complex or from the surface of the thylakoid membrane. 

It is possible that the 31 kD polypeptide shares some homology with an intrinsic, chlorophyll binding protein of similar MW observed in Prochloron and Cyanobacteria (5, 6). Details of the isolation and characteristics of this protein will be reported elsewhere. 

All P.p. are either hydrophobic, or they possess a strongly hydrophobic grouping, e.g. the phytol residue of chlorophyll. A simple model, in which P.p. are associated with the lipid layer of the thylakoid membrane, is however, unsatisfactory. It is necessary to propose a certain degree of ordered structure for P.p., and this is not possible if P.p. are subject to the random mobility of the lipid membrane components, as demanded by the fluid-mosaic model for membrane structure. Binding of a P. p. molecule to a protein would also be an unsatisfactory model, because the various P.p. would then be too widely separated for the efficient transfer of photons or resonance energy. A more feasible model would involve binding of several P. p. molecules to one protein, and there is much evidence for a system of this kind e.g. several chlorophyll-binding proteins have been isolated from... 

Tremolieres A, Dainese P, Bassi R. Heterogenous lipid distribution among chlorophyll-binding proteins of photosystem II in maize mesophyll chloroplasts. Eur J Biochem 1994 221 721-730. 

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