Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803.
In contrast to eukaryotes, most cyanobacteria contain several isoforms of the Rieske iron-sulfur protein, PetC, resulting in heterogeneity in the composition of the cytochrome b(6)f complexes. Of three isoforms in the mesophilic cyanobacterium Synechocystis PCC 6803, PetC1 is the major Rieske protein in the cytochrome b(6)f complex, whereas the physiological function of PetC2 and PetC3 is still uncertain. Comparison of wild type and various petC-deficient strains under selected light conditions revealed distinct functional differences: high-light exposure of wild type cells resulted in a significantly enhanced petC2 transcript level, whereas a Delta petC1 mutant showed a low cytochrome b(6)f content, low electron flux, and a considerably increased accumulation of cytochrome-bd oxidase. In contrast to wild type and Delta petC1, Delta petC2 and Delta petC3 strains still grew fast under high-light conditions although all three Rieske proteins are required for maximal electron transport rates. Although the presence of PetC3 appears to be required for activation of the cyclic electron transport, state transitions were more effective in the absence of PetC2 and/or PetC3. In summary, our data suggest defined roles of the various PetC proteins in short- and long-term light adaptation.
Tsunoyama
Yuichi
Y
Department of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany; Division of Biology, Radioisotope Research Center, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Bernát
Gábor
G
Department of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.
Dyczmons
Nina G
NG
Department of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany.
Schneider
Dirk
D
Department of Biochemistry and Molecular Biology, ZBMZ, Albert-Ludwigs-University Freiburg, 79104 Freiburg, Germany.
Rögner
Matthias
M
Department of Plant Biochemistry, Ruhr-University Bochum, 44780 Bochum, Germany. Electronic address: Matthias.Roegner@rub.de.
D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002734:Chlorophyll / Q000378:metabolism; D045346:Cytochrome b6f Complex / Q000378:metabolism; D004579:Electron Transport / Q000502:physiology; D014450:Electron Transport Complex III / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D008027:Light; D010084:Oxidation-Reduction; D010788:Photosynthesis / Q000502:physiology*; D010798:Phycocyanin / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D046939:Synechocystis / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D020033:Protein Isoforms; D021122:Protein Subunits; C037989:Rieske iron-sulfur protein; C002497:allophycocyanin; D010798:Phycocyanin; D002734:Chlorophyll; D045346:Cytochrome b6f Complex; D014450:Electron Transport Complex III
Microbiol Rev. 1993 Sep;57(3):725-49
8246846
J Biochem. 2009 Mar;145(3):395-401
19124292
Annu Rev Plant Biol. 2007;58:199-217
17201689
J Biol Chem. 2004 Oct 22;279(43):44621-7
15316016
EMBO J. 2001 Jul 16;20(14):3623-30
11447103
Photosynth Res. 2008 Feb-Mar;95(2-3):175-82
17922214
Biochim Biophys Acta. 2006 May-Jun;1757(5-6):362-8
16762315
Proc Natl Acad Sci U S A. 1997 Feb 18;94(4):1585-90
11038603
J Exp Bot. 2005 Jan;56(411):389-93
15582926
Plant Cell. 1999 Oct;11(10):2031-44
10521530
Plant Cell. 2006 Nov;18(11):3106-20
17114352
DNA Res. 1996 Jun 30;3(3):109-36
8905231
Biochim Biophys Acta. 1969 Feb 25;172(2):242-51
5775694
Res Microbiol. 2007 Jan-Feb;158(1):45-50
17224258
Nucleic Acids Res. 2002 May 1;30(9):e36
11972351
Nature. 1970 Aug 15;227(5259):680-5
5432063
Mol Cell Proteomics. 2002 Oct;1(10):816-27
12438564
Curr Opin Plant Biol. 1998 Jun;1(3):217-23
10066592
FEBS Lett. 2002 May 22;519(1-3):82-6
12023022
J Biol Chem. 2007 Feb 9;282(6):3730-7
17166849
Trends Plant Sci. 2004 Mar;9(3):130-7
15003236
Biochemistry. 2002 Mar 12;41(10):3422-9
11876651
J Biol Chem. 2002 Mar 29;277(13):10949-54
11788579
J Biol Chem. 1995 Oct 20;270(42):25225-32
7559660
Plant Cell Physiol. 2005 Aug;46(8):1433-6
15946981
EMBO Rep. 2002 Mar;3(3):280-5
11850400
Photosynth Res. 2004;82(3):327-38
16143844
Biochim Biophys Acta. 2009 Dec;1787(12):1479-85
19577535
J Biol Chem. 2001 May 18;276(20):16780-5
11278512
Photosynth Res. 1993 Jun;36(3):149-68
24318920
J Biol Chem. 2004 Sep 17;279(38):39383-8
15262969
J Struct Biol. 1998 Dec 15;124(2-3):311-34
10049814
Biochim Biophys Acta. 1969;189(3):366-83
5370012
J Biol Chem. 2003 Jun 6;278(23):20925-33
12672829
Annu Rev Biochem. 2006;75:769-90
16756511
Nucleic Acids Res. 2001 May 1;29(9):e45
11328886
Biochemistry. 1998 Dec 22;37(51):17944-51
9922162
EMBO J. 1999 Jun 1;18(11):2961-9
10357809
Photosynth Res. 2009 Mar;99(3):205-16
19137411
Plant Physiol. 2000 Feb;122(2):505-16
10677443
Mol Microbiol. 2008 Oct;70(1):140-50
18699865
Biochim Biophys Acta. 2007 Feb;1767(2):161-9
17274945
Biochim Biophys Acta. 2006 May-Jun;1757(5-6):339-45
16787635
Nature. 2004 Jun 3;429(6991):579-82
15175756
Biochim Biophys Acta. 2005 Nov 15;1710(1):1-12
16271700
EMBO J. 1994 Mar 1;13(5):1019-27
8131736
Plant Cell Environ. 2007 Sep;30(9):1041-51
17661746
J Biol Chem. 2001 Oct 12;276(41):38159-65
11483610
J Mol Endocrinol. 2002 Aug;29(1):23-39
12200227
Science. 2003 Mar 7;299(5612):1530-2
12624254
Photosynth Res. 2004;82(1):17-33
16228610
J Cell Biol. 1973 Aug;58(2):419-35
4199659
Trends Plant Sci. 2006 Jan;11(1):46-55
16352458
J Biol Chem. 1988 Oct 5;263(28):14334-42
2844767
Neurosci Lett. 2003 Mar 13;339(1):62-6
12618301