The FtsH protease slr0228 is important for quality control of photosystem II in the thylakoid membrane of Synechocystis sp. PCC 6803

Journal of Biological Chemistry

Volumn 281, Issue 2, 2006, Pages 1145-1151

  Komenda, Josef ^a,b   Barker, Myles ^c   Kuviková, Stanislava ^a,b   De Vries, Remco ^c   Mullineaux, Conrad W ^d   Tichý, Martin ^a,b   Nixon, Peter J ^c  

^a INSTITUTE OF MICROBIOLOGY   (Czech Republic)

^b UNIVERSITY OF SOUTH BOHEMIA   (Czech Republic)

^c IMPERIAL COLLEGE LONDON   (United Kingdom)

^d QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; FLUORESCENT LAMPS; GENES; IMMUNOLOGY; PROTEINS; REACTION KINETICS;

IMMUNOBLOTTING; PHOTODAMAGED PHOTOSYSTEM; SYNECHOCYSTIS SP. PCC 6803; THYLAKOID MEMBRANE;

BIOLOGICAL MEMBRANES;

CHLOROPHYLL A; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PROTEIN FTSH; PROTEIN SLR0228; PROTEINASE; UNCLASSIFIED DRUG; EPITOPE; METALLOPROTEINASE; PEPTIDE HYDROLASE;

ARTICLE; IMMUNOBLOTTING; IN VIVO STUDY; ISOTOPE LABELING; MUTAGENESIS; NONHUMAN; PHOTOSYSTEM II; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SYNECHOCYSTIS; THYLAKOID MEMBRANE; BIOCHEMISTRY; CELL MEMBRANE; CHEMISTRY; CHLOROPLAST; CONFOCAL MICROSCOPY; CYTOPLASM; GENOTYPE; LIGHT; METABOLISM; MISSENSE MUTATION; MUTATION; PHYSIOLOGY; PLASMID; PROTEIN BINDING; THYLAKOID; TIME; TWO DIMENSIONAL GEL ELECTROPHORESIS;

SYNECHOCYSTIS; SYNECHOCYSTIS SP.; SYNECHOCYSTIS SP. PCC 6803;

BIOCHEMISTRY; CELL MEMBRANE; CHLOROPLASTS; CYTOPLASM; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EPITOPES; GENOTYPE; GREEN FLUORESCENT PROTEINS; IMMUNOBLOTTING; LIGHT; METALLOENDOPEPTIDASES; MICROSCOPY, CONFOCAL; MUTATION; MUTATION, MISSENSE; PEPTIDE HYDROLASES; PHOTOSYSTEM II PROTEIN COMPLEX; PLASMIDS; PROTEIN BINDING; SYNECHOCYSTIS; THYLAKOIDS; TIME FACTORS;

EID: 33644867870     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M503852200     Document Type: Article

References (39)

1. Baumeister, W., Walz, J., Zühl, F., and Seemüller, E. (1998) Cell 92, 367-380
2. Adam, Z., and Clarke, A. K. (2002) Trends Plant Sci. 7, 451-456
3. Asada, K. (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. 50, 601-639
4. Prášil, O., Adir, N., and Ohad, I. (1992) in Topics in Photosynthesis (Barber, J., ed) Vol. 11, pp. 295-348, Elsevier, Amsterdam
5. Zouni, A., Witt H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W., and Orth, P. (2001) Nature 409, 739-743
6. Ferreira, K. N., Iverson, T. N., Maglaoui, K., Barber, J., and Iwata, S. (2004) Science 303, 1831-1838
7. Nixon, P.J., Barker, M., Boehm, M., de Vries, R., and Komenda, J. (2005) J. Exp. Bot. 56, 347-356
8. Langer, T. (2000) Trends Biochem. Sci. 25, 247-251
9. Tomoyasu, T., Yuki, T., Morimura, S., Mori, H., Yamanaka, K., Niki, H., Hiraga, S., and Ogura, T. (1993) J. Bacteriol. 175, 1344-1351
10. Krzywda, S., Brzozowski, A. M., Verma, C., Karata, K., Ogura, T., and Wilkinson, A. J. (2002) Structure (Camb.) 10, 1073-1083
11. Chiba, S., Akiyama, Y., and Ito, K. (2002) J. Bacteriol. 184, 4775-4782
12. Mann, N. H., Novac, N., Mullineaux, C. W., Newman, J., Bailey, S., and Robinson, C. (2000) FEBS Lett. 479, 72-77
13. Silva, P. A., Thompson, E., Bailey, S., Kruse, O., Mullineaux, C. W., Robinson, C., Mann, N. H., and Nixon, P. J. (2003) Plant Cell 15, 2152-2164
14. Zak, E., Norling, B., Maitra, R., Huang, F., Andersson, B., and Pakrasi, H. B. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 13443-13448
15. Jansen, T., Kanervo, E., Aro, E. M., and Maenpaa, P. (2002) J. Plant Physiol. 159, 1205-1211
16. Adam, Z., Zaltsman, A., Sinvany-Villalobo, G., and Sakamoto, W. (2005) Physiol. Plant. 123, 386-390
17. Bailey, S., Thompson, E., Nixon, P. J., Horton, P., Mullineaux, C. W., Robinson, C., and Mann, N. H. (2002) J. Biol. Chem. 277, 2006-2011
18. Sakamoto, W., Tamura, T., Hanba-Tomita, Y., Sodmergen, and Murata, M. (2002) Genes Cells 7, 769-780
19. Yu, F., Park, S., and Rodermel, S. (2004) Plant J. 37, 864-876
20. Ostersetzer, O., and Adam, Z. (1997) Plant Cell 9, 957-965
21. Vermaas, W. F., Ikeuchi, M., and Inoue, Y. (1988) Photosynth. Res. 17, 97-113
22. Williams, J. G. K. (1988) Methods Enzymol. 167, 766-778
23. Nixon, P. J., Trost, J. T., and Diner, B. A. (1992) Biochemistry 31, 10859-10871
24. Diner, B. A., Schlodder, E., Nixon, P. J., Coleman, W. J., Rappaport, F., Lavergne, J., Vermaas, W. F., and Chisholm, D. A. (2001) Biochemistry 40, 9265-9281
25. Pakrasi, H. B., Williams, J. G. K., and Arntzen, C. J. (1988) EMBO J. 7, 325-332
26. Kaltwasser, M., Wiegert, T., and Schumann, W. (2002) Appl. Environ. Microbiol. 268, 624-2628
27. Schmidt, T. G., Koepke, J., Frank, R., and Skerra, A. (1996) J. Mol. Biol. 255, 753-766
28. Komenda, J., Reisinger, V., Müller, B., Dobáková, M., Granvogl, B., and Eichacker, L. A. (2004) J. Biol. Chem. 279, 48620-48629
29. Tichý, M., Lupínková, L., Sicora, C., Vass, I., Kuviková, S., Prášil, O., and Komenda, J. (2003) Biochim. Biophys. Acta 1605, 55-66
30. Norling, B., Zak, E., Andersson, B., and Pakrasi, H. B. (1998) FEBS Lett. 436, 189-192
31. Huang, F., Parmryd, I., Nilsson, F., Persson, A., Pakrasi, H., Andersson, B., and Norling, B. (2002) Mol. Cell. Proteomics 1, 956-966
32. Zhang, P., Battchikova, N., Jansen, T., Appel, J., Ogawa, T., and Aro, E.-M. (2004) Plant Cell 16, 3326-3340
33. Spence, E. Sarcina, M., Ray, N., Møller, S. G., Mullineaux, C. W., and Robinson, C. (2003) Mol. Microbiol. 48, 1481-1489
34. Inagaki, N., Yamamoto, Y., and Satoh, K. (2001) FEBS Lett. 509, 197-201
35. Rögner, M., Chisholm, D. A., and Diner, B. A. (1991) Biochemistry 30, 5387-5395
36. Smith, D., and Howe, C. J. (1993) FEMS Microbiol. Lett. 110, 341-348
37. Zhang, L., Paakkarinen, V., Suorsa, M., and Aro, E. M. (2001) J. Biol. Chem. 276, 37809-37814
38. Anbudurai, P. R., Mor, T. S., Ohad, I., Shestakov, S. V., and Pakrasi, H. B. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 8082-8086
39. Keren, N., Liberton, M., and Pakrasi, H. B. (2005) J. Biol. Chem. 280, 6548-6553