The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

slr1739  -  similar to 13kD protein PsbW

Synechocystis sp. PCC 6803

This record was discontinued.
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of slr1739

 

High impact information on slr1739

  • To understand the regulatory mechanisms underlying the biogenesis of photosystem II (PSII) we have characterized the nuclear mutant hcf136 of Arabidopsis thaliana and isolated the affected gene [5].
  • Protein labelling studies in the presence of cycloheximide showed that the plastome-encoded PSII subunits are synthesized but are not stable [5].
  • During photosynthesis, the photosystem II (PSII) pigment-protein complex catalyzes oxygen evolution, a reaction in which a four-manganese ensemble plays a crucial role [6].
  • Cytochrome (cyt) b559, an integral membrane protein, is an essential component of the photosystem II (PSII) complex in the thylakoid membranes of oxygenic photosynthetic organisms [1].
  • A secondary effect of such a structural change was that D1 and D2, two proteins that form the catalytic core (reaction center) of PSII, were also destabilized [1].
 

Chemical compound and disease context of slr1739

  • Mutants of the cyanobacterium Synechocystis sp. Pasteur Culture Collection (PCC) 6803 that specifically lack the extrinsic 33-kDa manganese-stabilizing polypeptide of the photosystem II oxygen-evolving complex have been constructed by two independent methods [7].
  • To understand the function of the dark stable tyrosine radical, D+, we have characterized two site-directed mutations at the D tyrosine residue in the transformable cyanobacterium, Synechocystis sp. PCC 6803, through the use of purified photosystem II particles (Noren, G. H., Boerner, R. J., and Barry, B. A. (1991) Biochemistry 30, 3943-3950) [8].
  • Inactivation of the open reading frame slr0399 in Synechocystis sp. PCC 6803 functionally complements mutations near the Q(A) niche of photosystem II. A possible role of Slr0399 as a chaperone for quinone binding [9].
  • Construction and characterization of genetically modified synechocystis sp. PCC 6803 photosystem II core complexes containing carotenoids with shorter pi-conjugation than beta-carotene [10].
  • Structure-based kinetic modeling of excited-state transfer and trapping in histidine-tagged photosystem II core complexes from synechocystis [11].
 

Biological context of slr1739

 

Anatomical context of slr1739

 

Associations of slr1739 with chemical compounds

  • A cluster of manganese, calcium, and chloride ions, whose binding environment is optimized by PSII extrinsic proteins, catalyzes this water-splitting reaction [2].
  • The involvement of Phe255, Ser264, and Leu271 of D1 in plastoquinone binding and electron transfer in PSII was established [19].
  • Besides chlorophyll and quinone, photosystem II contains other organic cofactors, including two known as Z and D. Z transfers electrons from the site of water oxidation to the oxidized reaction center primary donor, P+.680, while D+. gives rise to the dark-stable EPR spectrum known as signal II [16].
  • Measurements of thermoluminescence profiles and rates of reduction of 2,6-dichlorophenolindophenol indicated that PSII complexes in the mutant cells had functional reaction centers that were unable to accept electrons from water [20].
  • We suggest that the C2 symmetry in photosystem II extends beyond P680 to its immediate electron donor and conclude that Z is Tyr-161 of the D1 polypeptide [16].
 

Physical interactions of slr1739

  • Taken together, these results indicate that the cytochrome c-550 is transported into the thylakoid lumen and contributes to optimal functional stability of photosystem II in cyanobacteria [21].
  • Deletion of slr0286 did not affect photoautotrophic capacity in wild type but led to a marked decrease in the apparent affinity of Ca(2+) to its binding site at the water-splitting system of photosystem II and to a reduced heat tolerance of the oxygen-evolving system, particularly in E69Q [22].
  • Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC 6803 [23].
 

Regulatory relationships of slr1739

 

Other interactions of slr1739

 

Analytical, diagnostic and therapeutic context of slr1739

  • To investigate the influence of these His residues on the structure of cyt b559 and the PSII complex, we used a site directed mutagenesis approach to replace each His residue with a Leu residue [1].
  • Atrazine bindng and Western blot analysis showed that these mutants on a per-chlorophyll basis contained 53-67% of the amount of photosystem II as compared with wild type [21].
  • The PS II core complex has an apparent molecular mass of 310 +/- 20 kDa (including the detergent shell); subunits of 43, 37, 33, 29, and 10-11 kDa were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting [30].
  • Changes in structural and functional properties of oxygen-evolving complex induced by replacement of D1-glutamate 189 with glutamine in photosystem II: ligation of glutamate 189 carboxylate to the manganese cluster [31].
  • The interaction of ScpDHis with PsbH and CP47 was further confirmed by electron microscopy of PSII labeled with Ni-NTA Nanogold [32].

References

  1. Site directed mutagenesis of the heme axial ligands of cytochrome b559 affects the stability of the photosystem II complex. Pakrasi, H.B., De Ciechi, P., Whitmarsh, J. EMBO J. (1991) [Pubmed]
  2. Homologs of plant PsbP and PsbQ proteins are necessary for regulation of photosystem ii activity in the cyanobacterium Synechocystis 6803. Thornton, L.E., Ohkawa, H., Roose, J.L., Kashino, Y., Keren, N., Pakrasi, H.B. Plant Cell (2004) [Pubmed]
  3. Psb29, a conserved 22-kD protein, functions in the biogenesis of Photosystem II complexes in Synechocystis and Arabidopsis. Keren, N., Ohkawa, H., Welsh, E.A., Liberton, M., Pakrasi, H.B. Plant Cell (2005) [Pubmed]
  4. Two redox-active beta-carotene molecules in photosystem II. Tracewell, C.A., Brudvig, G.W. Biochemistry (2003) [Pubmed]
  5. A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana. Meurer, J., Plücken, H., Kowallik, K.V., Westhoff, P. EMBO J. (1998) [Pubmed]
  6. Molecular identification of an ABC transporter complex for manganese: analysis of a cyanobacterial mutant strain impaired in the photosynthetic oxygen evolution process. Bartsevich, V.V., Pakrasi, H.B. EMBO J. (1995) [Pubmed]
  7. Construction and characterization of cyanobacterial mutants lacking the manganese-stabilizing polypeptide of photosystem II. Philbrick, J.B., Diner, B.A., Zilinskas, B.A. J. Biol. Chem. (1991) [Pubmed]
  8. Removal of stable tyrosine radical D+ affects the structure or redox properties of tyrosine Z in manganese-depleted photosystem II particles from Synechocystis 6803. Boerner, R.J., Bixby, K.A., Nguyen, A.P., Noren, G.H., Debus, R.J., Barry, B.A. J. Biol. Chem. (1993) [Pubmed]
  9. Inactivation of the open reading frame slr0399 in Synechocystis sp. PCC 6803 functionally complements mutations near the Q(A) niche of photosystem II. A possible role of Slr0399 as a chaperone for quinone binding. Ermakova-Gerdes, S., Vermaas, W. J. Biol. Chem. (1999) [Pubmed]
  10. Construction and characterization of genetically modified synechocystis sp. PCC 6803 photosystem II core complexes containing carotenoids with shorter pi-conjugation than beta-carotene. Bautista, J.A., Tracewell, C.A., Schlodder, E., Cunningham, F.X., Brudvig, G.W., Diner, B.A. J. Biol. Chem. (2005) [Pubmed]
  11. Structure-based kinetic modeling of excited-state transfer and trapping in histidine-tagged photosystem II core complexes from synechocystis. Vassiliev, S., Lee, C.I., Brudvig, G.W., Bruce, D. Biochemistry (2002) [Pubmed]
  12. Targeted mutagenesis of the psbE and psbF genes blocks photosynthetic electron transport: evidence for a functional role of cytochrome b559 in photosystem II. Pakrasi, H.B., Williams, J.G., Arntzen, C.J. EMBO J. (1988) [Pubmed]
  13. Molecular analysis of a mutant defective in photosynthetic oxygen evolution and isolation of a complementing clone by a novel screening procedure. Dzelzkalns, V.A., Bogorad, L. EMBO J. (1988) [Pubmed]
  14. Activation of the silent psbA1 gene in the cyanobacterium Synechocystis sp strain 6803 produces a novel and functional D1 protein. Salih, G.F., Jansson, C. Plant Cell (1997) [Pubmed]
  15. Inactivation of a Synechocystis sp strain PCC 6803 gene with homology to conserved chloroplast open reading frame 184 increases the photosystem II-to-photosystem I ratio. Wilde, A., Härtel, H., Hübschmann, T., Hoffmann, P., Shestakov, S.V., Börner, T. Plant Cell (1995) [Pubmed]
  16. Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system. Debus, R.J., Barry, B.A., Babcock, G.T., McIntosh, L. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  17. Photochemical competence of assembled photosystem II core complex in cyanobacterial plasma membrane. Keren, N., Liberton, M., Pakrasi, H.B. J. Biol. Chem. (2005) [Pubmed]
  18. Isolation of a highly active photosystem II preparation from Synechocystis 6803 using a histidine-tagged mutant of CP 47. Bricker, T.M., Morvant, J., Masri, N., Sutton, H.M., Frankel, L.K. Biochim. Biophys. Acta (1998) [Pubmed]
  19. Mutations in the D1 subunit of photosystem II distinguish between quinone and herbicide binding sites. Ohad, N., Hirschberg, J. Plant Cell (1992) [Pubmed]
  20. The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex. Anbudurai, P.R., Mor, T.S., Ohad, I., Shestakov, S.V., Pakrasi, H.B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  21. The role of cytochrome c-550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803. Shen, J.R., Vermaas, W., Inoue, Y. J. Biol. Chem. (1995) [Pubmed]
  22. A novel protein involved in the functional assembly of the oxygen-evolving complex of photosystem II in Synechocystis sp. PCC 6803. Kufryk, G.I., Vermaas, W.F. Biochemistry (2001) [Pubmed]
  23. Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC 6803. Komenda, J., Lupínková, L., Kopecký, J. Eur. J. Biochem. (2002) [Pubmed]
  24. Genetic and immunological analyses of the cyanobacterium Synechocystis sp. PCC 6803 show that the protein encoded by the psbJ gene regulates the number of photosystem II centers in thylakoid membranes. Lind, L.K., Shukla, V.K., Nyhus, K.J., Pakrasi, H.B. J. Biol. Chem. (1993) [Pubmed]
  25. Photosystem II assembly in CP47 mutant of Synechocystis sp. PCC 6803 is dependent on the level of chlorophyll precursors regulated by ferrochelatase. Sobotka, R., Komenda, J., Bumba, L., Tichy, M. J. Biol. Chem. (2005) [Pubmed]
  26. Cloning of the psbK gene from Synechocystis sp. PCC 6803 and characterization of photosystem II in mutants lacking PSII-K. Ikeuchi, M., Eggers, B., Shen, G.Z., Webber, A., Yu, J.J., Hirano, A., Inoue, Y., Vermaas, W. J. Biol. Chem. (1991) [Pubmed]
  27. Analysis of the psbU gene encoding the 12-kDa extrinsic protein of photosystem II and studies on its role by deletion mutagenesis in Synechocystis sp. PCC 6803. Shen, J.R., Ikeuchi, M., Inoue, Y. J. Biol. Chem. (1997) [Pubmed]
  28. Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease. Analysis of a spontaneous photosystem II-deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803. Shestakov, S.V., Anbudurai, P.R., Stanbekova, G.E., Gadzhiev, A., Lind, L.K., Pakrasi, H.B. J. Biol. Chem. (1994) [Pubmed]
  29. UV-B radiation induced exchange of the D1 reaction centre subunits produced from the psbA2 and psbA3 genes in the Cyanobacterium synechocystis sp. PCC 6803. Vass, I., Kirilovsky, D., Perewoska, I., Máté, Z., Nagy, F., Etienne, A.L. Eur. J. Biochem. (2000) [Pubmed]
  30. Purification and characterization of photosystem I and photosystem II core complexes from wild-type and phycocyanin-deficient strains of the cyanobacterium Synechocystis PCC 6803. Rögner, M., Nixon, P.J., Diner, B.A. J. Biol. Chem. (1990) [Pubmed]
  31. Changes in structural and functional properties of oxygen-evolving complex induced by replacement of D1-glutamate 189 with glutamine in photosystem II: ligation of glutamate 189 carboxylate to the manganese cluster. Kimura, Y., Mizusawa, N., Ishii, A., Nakazawa, S., Ono, T.A. J. Biol. Chem. (2005) [Pubmed]
  32. Cyanobacterial Small Chlorophyll-binding Protein ScpD (HliB) Is Located on the Periphery of Photosystem II in the Vicinity of PsbH and CP47 Subunits. Promnares, K., Komenda, J., Bumba, L., Nebesarova, J., Vacha, F., Tichy, M. J. Biol. Chem. (2006) [Pubmed]
 
WikiGenes - Universities