ИЗУЧЕНИЕ СТРУКТУРНОГО ЭЛЕМЕНТА БЕЛКА D1-209, УЧАСТВУЮЩЕГО В ФУНКЦИОНАЛЬНОЙ СБОРКЕ ПРОТЕИНОВОГО КОМПЛЕКСА ФОТОСИСТЕМЫ 2
Ключевые слова:
фотосинтез, реакционный центр, фотосистема 2, комбинаторный мутагенез, функциональная сборка белков
Аннотация
Структурные элементы (сайты) ключевого белка фотосистемы 2 (ФС2) D1-208, D1-209 и D1-212 вместе с еще тремя аминокислотными (АК) остатками составляют мотив, подобный Гли-xxx-Гли (D1-Гли208-ххх-Сер212), который расположен на спирали D на участке тесного контакта белковых субъединиц D1/D2 комплекса ФС2. Мы предположили, что один из АК-остатков этого мотива D1-209 может участвовать в функциональной сборке протеинового комплекса ФС2. Чтобы проверить эту гипотезу и выяснить молекулярные механизмы, лежащие в основе функции ФС2, был выполнен комбинаторный мутагенез на сайте D1-209 в цианобактериях Synechocystis PCC 6803. В результате мутагенеза и функциональных измерений мы выяснили, что в сайте 209 белка D1 вместо Сер (дикий тип) могут быть вставлены малые АК-остатки (Гли и Ала), которые функционируют подобно Сер. Однако средние по размеру АК-остатки (Цис, Тре, Про, Асн, Асп и Вал) значительно нарушают нормальные функции протеинового комплекса ФС2.
Литература
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2. Ferroni L. Photosynthetic acclimation to the light environment: molecular mechanisms to understand plant consortia // J Ecosys. Ecograph. 2012. N 2(1). P. 1-2.
3. Umena Y., Kawakami K., Shen J.R., Kamiya N. Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A // Nature. 2011. N 473. Р. 55-60.
4. Cardona T., Sedoud A., Cox N., Rutherford A.W. Charge separation in photosystem II: a comparative and evolutionary overview // Biochim. Biophys. Acta. 2012. N 1817(1). P. 26-43.
5. Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W. Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride // Nat. Struct. Mol. Biol. 2009. N 16(3). P. 334-342.
6. Koua F.H., Umena Y., Kawakami K., Shen J.R. Structure of Sr-substituted photosystem II at 2.1 A resolution and its implications in the mechanism of water oxidation // Proc. Natl. Acad. Sci. USA. 2013. N 110 (10). P. 3889-3894.
7. Maxam A.M., Gilbert W. A new method of sequencing DNA // Proc. Natl. Acad. Sci. USA. 1977. N 74. P. 560-564.
8. Rosenblum B.B., Lee L.G., Spurgeon S.L., Khan S.H., Menchen S.M., Heiner C.R., Chen S.M. New dye-labeled terminators for improved DNA sequencing patterns // Nucleic Acids Res. 1997. N 25 (22). P. 4500-4504.
9. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice // Nucleic Acids Res. 1994. N 22. P. 4673-4680.
10. Curran A.R., Engelman D.M. Sequence motifs, polar interactions and conformational changes in helical membrane proteins // Curr. Opin. Struct. Biol. 2003. N 1. P. 412-417.
11. Logothetis D.E., Lupyan D., Rosenhouse-Dantsker A. Diverse Kir modulators act in close proximity to residues implicated in phosphoinositide binding // J Physiol. 2007. N 582. P. 953-965.
12. Choi M.Y., Cardarelli L., Therien A.G., Deber C.M. Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations // Biochemistry. 2004. N 43. P. 8077-8083.
13. Choma C., Gratkowski H., Lear J.D., DeGrado W.F. Asparagine-mediated self-association of a model transmembrane helix // Nat. Struct. Biol. 2000. N 7. P. 161-166.
14. Therien A.G., Grant F.E., Deber C.M. Interhelical hydrogen bonds in the CFTR membrane domain // Nat. Struct. Biol. 2001. N 8 (7). P. 597-601.
15. Shlyk-Kerner O., Samish I., Kaftan D., Holland N., Sai M., Kless H., Scherz A. Modulation of protein flexibility acclimatizes photosynthetic energy conversion to the ambient temperature // Nature. 2006. N 442. P. 827-830.
16. Dinamarca J., Shlyk-Kerner O., Kaftan D., Goldberg E., Dulebo A., Gidekel M., Gutierrez A., Scherz A. Double mutation in photosystem II reaction centers and elevated CO2 grant thermotolerance to mesophilic cyanobacterium // PLoS One. 2011. N 6 (12). Р. 1-13.
17. Senes A., Engel D.E., DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs // Curr. Opin. Struct. Biol. 2004. N 14. P. 465-479.
18. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling // Electrophoresis. 1997. N 18. Р. 2714-2723.
19. Kaneko T. et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions // DNA Res. 1996. N 3. P.109-136.
20. Kless H., Vermaas W. Combinatorial mutagenesis and structural simulations in the environment of the redox-active tyrosine YZ of photosystem II // Biochem. 1996. Vol. 35. P. 16458-16464.
21. Williams J.G.K. Construction of specific mutations in Photosystem II Photosynthetic Reaction Center by genetic engineering methods in Synechocystis 6803 // Methods in enzymology. 1988. N 167. P. 766-778.
22. Kerner O. The contribution of small amino acids at the D1/D2 interface to the functional flexibility and temperature adaptation of photosystem II reaction center: PhD dissertation. Rehovot, Israel: Weizmann Institute of Science, 2006. 106 p.
23. Rippka R., Deruelles J., Waterbury J., Herdman M., Stanier R. Generic assignments, strain histories and properties of pure cultures of cyanobacteria // J. Gen. Microbiol. 1979. N 111. P. 1-61.
24. Lichtenthaler H.K., Wellburn A.R. Determinations of total carotenoids and chlorophylls a and b of leaf extracts in different solvents // Biochem. Soc. Transactions. 1983. N 11. P. 591-592.
25. Gilmore A.M., Hazlett T.L., Debrunner P.G., Govindjee. Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: Photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence // Photosynth. Res. 1996. N 48. P. 171-187.
26. Callahan F.E., Ghirardi M.L., Sopory S.K., Mehta A.M., Edelmanl M., Mattoo A.K. A novel metabolic form of the 32 kDa-D1 protein in the grana-localized reaction center of photosystem II // J Biol. Chem. 1990. N 265. P. 15357-15360.
27. Sicora C., Wiklund R., Jansson C., Vass I. Charge stabilization and recombination in Photosystem II containing the D1 protein product of the psbA1 gene in Synechocystis 6803 // Phys. Chem. Chemical Phys. 2004. N 6. P. 4832-4837.
28. Шлык О.В., Кафтан Д., Шерц А. О роли глицина в регуляции скорости переноса электронов в реакционном центре фотосистемы II // Вестн. Удм. ун-та. Сер. Биология. Науки о Земле. 2013. № 1. С. 52-59.
29. Mohamed H.E., van de Meene A.M., Roberson R.W., Vermaas, W.F. Myxoxanthophyll is required for normal cell wall structure and thylakoid organization in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol. 2005. N 187. P. 6883-6892.
30. Zamyatnin A.A. Protein volume in solution // Prog. Biophys. Mol. Biol. 1972. N 24. P. 107-123.
Поступила в редакцию
2014-12-09
Опубликована 2015-03-25
Опубликована 2015-03-25