@article{shi_low_2004,
	title = {The low molecular mass subunits of the photosynthetic supracomplex, photosystem {II}},
	volume = {1608},
	issn = {0005-2728},
	doi = {10.1016/j.bbabio.2003.12.004},
	abstract = {The photosystem II (PSII) complex is located in the thylakoid membrane of higher plants, algae and cyanobacteria and drives the water oxidation process of photosynthesis, which splits water into reducing equivalents and molecular oxygen by solar energy. Electron and X-ray crystallography analyses have revealed that the PSII core complex contains between 34 and 36 transmembrane CL-helices, depending on the organism. Of these helices at least 12-14 are attributed to low molecular mass proteins. However, to date, at least 18 low molecular mass ({\textless} 10 kDa) subunits are putatively associated with the PSII complex. Most of them contain a single transmembrane span and their protein sequences are conserved among photosynthetic organisms. In addition, these proteins do not have any similarity to any known functional proteins in any type of organism, and only two of them bind a cofactor. These findings raise intriguing questions about why there are so many small protein subunits with single-transmembrane spans in the PSII complex, and their possible functions. This article reviews our current knowledge of this group of proteins. Deletion mutations of the low molecular mass subunits from both prokaryotic and eukaryotic model systems are compared in an attempt to understand the function of these proteins. From these comparisons it seems that the majority of them are involved in stabilization, assembly or dimerization of the PSII complex. The small proteins may facilitate fast dynamic conformational changes that the PSII complex needs to perform an optimal photosynthetic activity. (C) 2004 Elsevier B.V. All rights reserved.},
	language = {English},
	number = {2-3},
	journal = {Biochimica Et Biophysica Acta-Bioenergetics},
	author = {Shi, L. X. and Schroder, W. P.},
	month = feb,
	year = {2004},
	note = {Place: Amsterdam
Publisher: Elsevier Science Bv
WOS:000220012300001},
	keywords = {Arabidopsis, Synechocystis, arabidopsis-thaliana, center core   complex, cyanobacterium synechococcus-elongatus, function, light-harvesting antenna, open reading frames, ps2, psii-h subunit, reaction-center complex, sec-independent insertion, small protein, synechocystis sp pcc-6803, thylakoid   membrane-proteins},
	pages = {75--96},
}

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However, to date, at least 18 low molecular mass (\\textless 10 kDa) subunits are putatively associated with the PSII complex. Most of them contain a single transmembrane span and their protein sequences are conserved among photosynthetic organisms. In addition, these proteins do not have any similarity to any known functional proteins in any type of organism, and only two of them bind a cofactor. These findings raise intriguing questions about why there are so many small protein subunits with single-transmembrane spans in the PSII complex, and their possible functions. This article reviews our current knowledge of this group of proteins. Deletion mutations of the low molecular mass subunits from both prokaryotic and eukaryotic model systems are compared in an attempt to understand the function of these proteins. From these comparisons it seems that the majority of them are involved in stabilization, assembly or dimerization of the PSII complex. The small proteins may facilitate fast dynamic conformational changes that the PSII complex needs to perform an optimal photosynthetic activity. (C) 2004 Elsevier B.V. All rights reserved.","language":"English","number":"2-3","journal":"Biochimica Et Biophysica Acta-Bioenergetics","author":[{"propositions":[],"lastnames":["Shi"],"firstnames":["L.","X."],"suffixes":[]},{"propositions":[],"lastnames":["Schroder"],"firstnames":["W.","P."],"suffixes":[]}],"month":"February","year":"2004","note":"Place: Amsterdam Publisher: Elsevier Science Bv WOS:000220012300001","keywords":"Arabidopsis, Synechocystis, arabidopsis-thaliana, center core complex, cyanobacterium synechococcus-elongatus, function, light-harvesting antenna, open reading frames, ps2, psii-h subunit, reaction-center complex, sec-independent insertion, small protein, synechocystis sp pcc-6803, thylakoid membrane-proteins","pages":"75–96","bibtex":"@article{shi_low_2004,\n\ttitle = {The low molecular mass subunits of the photosynthetic supracomplex, photosystem {II}},\n\tvolume = {1608},\n\tissn = {0005-2728},\n\tdoi = {10.1016/j.bbabio.2003.12.004},\n\tabstract = {The photosystem II (PSII) complex is located in the thylakoid membrane of higher plants, algae and cyanobacteria and drives the water oxidation process of photosynthesis, which splits water into reducing equivalents and molecular oxygen by solar energy. Electron and X-ray crystallography analyses have revealed that the PSII core complex contains between 34 and 36 transmembrane CL-helices, depending on the organism. Of these helices at least 12-14 are attributed to low molecular mass proteins. However, to date, at least 18 low molecular mass ({\\textless} 10 kDa) subunits are putatively associated with the PSII complex. Most of them contain a single transmembrane span and their protein sequences are conserved among photosynthetic organisms. In addition, these proteins do not have any similarity to any known functional proteins in any type of organism, and only two of them bind a cofactor. These findings raise intriguing questions about why there are so many small protein subunits with single-transmembrane spans in the PSII complex, and their possible functions. This article reviews our current knowledge of this group of proteins. Deletion mutations of the low molecular mass subunits from both prokaryotic and eukaryotic model systems are compared in an attempt to understand the function of these proteins. From these comparisons it seems that the majority of them are involved in stabilization, assembly or dimerization of the PSII complex. The small proteins may facilitate fast dynamic conformational changes that the PSII complex needs to perform an optimal photosynthetic activity. (C) 2004 Elsevier B.V. All rights reserved.},\n\tlanguage = {English},\n\tnumber = {2-3},\n\tjournal = {Biochimica Et Biophysica Acta-Bioenergetics},\n\tauthor = {Shi, L. X. and Schroder, W. 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