Association of the 17-kDa extrinsic protein with photosystem II in higher plants

Biochemistry

Volumn 44, Issue 46, 2005, Pages 15216-15221

  Meades Jr , Glen D ^a   McLachlan, Anne ^b   Sallans, Larry ^b   Limbach, Patrick A ^b   Frankel, Laurie K ^a   Bricker, Terry M ^a  

^a LOUISIANA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF CINCINNATI   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; ENZYMES; LIQUID CHROMATOGRAPHY; PHOTOCHEMICAL REACTIONS; PLANTS (BOTANY);

IONIC INTERFERENCE; PEPTIDES; PHOTOSYSTEM II; SPINACH;

PROTEINS;

PEPTIDE FRAGMENT; PROTEINASE; UNCLASSIFIED DRUG; V8 PROTEASE; VEGETABLE PROTEIN;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; BIOTINYLATION; NONHUMAN; PHOTOSYSTEM II; PLANT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; STAPHYLOCOCCUS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BIOTIN; BIOTINYLATION; LYSINE; PHOTOSYSTEM II PROTEIN COMPLEX; PLANT PROTEINS; SERINE ENDOPEPTIDASES; SPINACIA OLERACEA; SUCCINIMIDES; TRYPSIN;

EMBRYOPHYTA; SPINACIA OLERACEA; STAPHYLOCOCCUS;

EID: 27944461037     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051704u     Document Type: Article

References (34)

1. Bricker, T. M., and Ghanotakis, D. (1996) The structure and function of the oxygen-evolving complex, in Advances in Photosynthesis. Oxygenic Photosynthesis: The Light Reactions (Yocum, C. F., and Ort, D. R., Eds.) Vol. 4, pp 113-136.
2. Kuwabara, T., and Murata, N. (1982) Inactivation of photosynthetic oxygen evolution and concomitant release of three polypeptides in the photosystem II particles of spinach chloroplasts, Plant Cell Physiol. 23, 533-539.
3. Akerlund, H.-E., Jannson, C., and Andersson, B. (1982) Reconstitution of oxygen evolution in high salt washed photosystem II particles, Biochim. Biophys. Acta 681, 1-10.
4. Ghanotakis, D. F., Babcock, G. T., and Yocum, C. F. (1984) Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations, FEBS Lett. 167, 127-130.
5. - with 18-kDa, 24-kDa, and 33-kDa proteins, FEBS Lett. 180, 303-308.
6. Yamamoto, Y., and Kubota, F. (1987) Specific release of the extrinsic 18 kDa protein from spinach photosystem II particles by the treatment with NaCl and methanol and its application for large-scale purification of the three extrinsic proteins of photosystem II without chromatography, Biochim. Biophys. Acta 893, 579-583.
7. 2-evolving PS II particles by divalent salt-washing, FEBS Lett. 164, 255-260.
8. Miyao, M., and Murata, N. (1984) Role of the 33 kDa polypeptide in preserving Mn in the photosynthetic oxygen-evolution, FEBS Lett. 170, 350-354.
9. Bricker, T. M. (1992) Oxygen evolution in the absence of the 33 kDa manganese-stabilizing protein, Biochemistry 31, 4623-4628.
10. 2 evolution, Biochemistry 30, 440-446.
11. Miyao, M., and Murata, N. (1983) Partial disintegration and reconstitution of the photosynthetic oxygen evolution complex, Biochim. Biophys. Acta 725, 87-93.
12. Calderone, V. T., Vujicic, A. M., Battistutta, R., Giacometti, G. M., Andreucci, F., Barbato, R., Zanotti, G. (2003) Crystal structure of the PsbQ protein of photosystem II from higher plants, EMBO Rep. 900-905.
13. Hermoso, J. A., Baisera, M., de las Rivas, J., and Arellano, J. (2004) Crystal structure of the 16 kDa protein from higher plants, PDB accession IVYK.
14. Kuwabara, T., Murata, T., Miyao, M., and Murata, N. (1986) Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex a study of a binding site, Biochim. Biophys. Acta 850, 146-155.
15. Kuwabara, T., and Suzuki, K. (1994) A prolyl endoproteinase that acts specifically on the extrinsic 18 kDa protein of photosystem II: Purification and further characterization, Plant Cell Physiol. 35, 665-675.
16. Bricker, T. M., Pakrasi, H. B., and Sherman, L. A. (1985) Characterization of a spinach photosystem II core preparation isolated by a simplified method, Biochim. Biophys. Acta 237, 170-176.
17. Arnon, D. I. (1949) Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris, Plant Physiol. 24, 1-15.
18. Berthold, D. A., Babcock, G. T., and Yocum, C. F. (1981) A highly resolved oxygen-evolving photosystem II preparations from spinach thylakoid membranes, FEBS Lett. 134, 231-234.
19. Ghanotakis, D. F., and Babcock, G. T. (1983) Hydroxylamine as an inhibitor between Z and P680 in photosystem II, FEBS Lett. 153, 231-234.
20. Delepelaire, P., and Chua, N. (1979) Lithium dodecyl sulfate/ polyacrylamide gel electrophoresis of thylakoid membranes at 4 °C: Characterizations of two additional chlorophyll a-protein complexes, Proc. Natl. Acad. Sci. U.S.A. 76, 111-115.
21. Frankel, L. K., and Bricker, T. M. (1990) Monoclonal antibodies directed against the 33, 24, and 17 kDa extrinsic proteins of spinach photosystem II, in Current Research in Photosynthesis (Batcheffsky, M., Ed.) pp 825-828.
22. Bricker, T. M., Odom, W. R., and Queirolo, C. B. (1988) Close association of the 33 kDa extrinsic protein with the apoprotein of CPa-1 in photosystem II, FEBS Lett. 231, 111-117.
23. Miyao, M., Fujimura, Y., and Murata, N. (1988) Partial degradation of the extrinsic 23 kDa protein of the photosystem II complex of spinach, Biochim. Biophys. Acta 936, 465-474.
24. Yamamoto, Y., and Kubota, F. (1987) Specific release of the extrinsic 18-kDa protein from spinach photosystem II particles by the treatment with NaCl and methanol and its application for large scale purification of the three extrinsic proteins of photosystem II without chromatography, Biochim. Biophys. Acta 893, 579-583.
25. Xu, Q. A., and Bricker, T. M. (1992) Structural organization of proteins on the oxidizing side of photosystem II: Two molecules of the 33 kDa manganese-stabilizing protein per reaction center, J. Biol. Chem. 267, 25816-25821.
26. Stone, K. L., LoPresti, M. B., Crawford, J. M., DeAngelis, R., and Williams, K. R. (1989) Enzymatic digestion of proteins and HPLC peptide isolation, in A Practical Guide to Protein and Peptide Purification for Microsequencing (Matsudaira, P. T., Ed.) pp 31-47.
27. Frankel, L., and Bricker, T. M. (1995) Interaction of the 33-kDa extrinsic protein with photosystem II: Identification of domains on the 33-kDa protein that are shielded from NHS-biotinylation by photosystem II, Biochemistry 34, 7492-7497.
28. Miura, T., Shen, J.-R., Takahashi, S., Kamo, M., Nakamura, E., Ohta, H., Kamei, A., Inoue, Y., Domae, N., Takio, K., Nakazato, K., Inoue, Y., and Enami, I. (1997) Identification of domains on the extrinsic 33-kDa protein possibly involved in electrostatic interaction with photosystem II complex by means of chemical modification, J. Biol. Chem. 272, 3788-3798.
29. Bricker, T. M., and Frankel, L. K. (2003) Carboxylate groups on the manganese-stabilizing protein are required for efficient binding of the 24 kDa protein to photosystem II, Biochemistry 42, 2056-2061.
30. Andersson, B., Larsson, C., Jansson, C., Ljungberg, U., and Akerlund, H.-E. (1984) Immunological studies on the organization of proteins in photosynthetic oxygen evolution, Biochim. Biophys. Acta 766, 21-26.
31. Kavelaki, K., and Ghanotakis, D. F. (1991) Effects of the manganese complex on the binding of the extrinsic proteins (17, 23, and 33 kDa) of photosystem II, Photosynth. Res. 29, 149-155.
32. Enami, I., Mochizuki, Y., Takahashi, S., Kakuno, T., Horio, T., Satoh, K., and Katoh, S. (1990) Evidence from crosslinking for the nearest neighbor relationships among the three extrinsic proteins of spinach photosystem II complexes that are associated with oxygen evolution, Plant Cell Physiol. 31, 725-729.
33. Enami, I., Yoshihara, S., Tohri, A., Okumura, A., Ohta, H., and Shen, J. R. (2000) Cross-reconstitution of various extrinsic proteins and photosystem II complexes from cyanobacteria, red algae, and higher plants, Plant Cell Physiol. 41, 1354-1364.
34. Suzuki, T., Minagawa, J., Tomo, T., Sonoike, K., Ohta, H., and Enami, I. (2003) Binding and functional properties of the extrinsic proteins in oxygen-evolving photosystem II particles fram a green alga, Chlamydomonas reinhardtii having His-tagged CP47, Plant Cell Physiol. 44, 76-84.