Further characterization of the psbH locus of Synechocystis sp. PCC 6803: Inactivation of psbH impairs QA to QB electron transport in photosystem 2

Biochemistry ◽  
1993 ◽  
Vol 32 (6) ◽  
pp. 1454-1465 ◽  
Author(s):  
Steve R. Mayes ◽  
James M. Dubbs ◽  
Imre Vass ◽  
Eva Hideg ◽  
Laszlo Nagy ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem 2 ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals Cloning of the psbK gene from Synechocystis sp. PCC 6803 and characterization of photosystem II in mutants lacking PSII-K

1991 ◽  
Vol 266 (17) ◽  
pp. 11111-11115
Author(s):  
M. Ikeuchi ◽  
B. Eggers ◽  
G.Z. Shen ◽  
A. Webber ◽  
J.J. Yu ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals Recombinant Deg/HtrA proteases from Synechocystis sp. PCC 6803 differ in substrate specificity, biochemical characteristics and mechanism

2011 ◽  
Vol 435 (3) ◽  
pp. 733-742 ◽  
Author(s):  
Pitter F. Huesgen ◽  
Helder Miranda ◽  
XuanTam Lam ◽  
Manuela Perthold ◽  
Holger Schuhmann ◽  
...  
Keyword(s):  
Serine Proteases ◽  
Protein Quality ◽  
Biochemical Characterization ◽  
Pdz Domain ◽  
Control Mechanisms ◽  
Ph Optimum ◽  
Periplasmic Proteins ◽  
Synechocystis Sp ◽  
Pcc 6803

Cyanobacteria require efficient protein-quality-control mechanisms to survive under dynamic, often stressful, environmental conditions. It was reported that three serine proteases, HtrA (high temperature requirement A), HhoA (HtrA homologue A) and HhoB (HtrA homologue B), are important for survival of Synechocystis sp. PCC 6803 under high light and temperature stresses and might have redundant physiological functions. In the present paper, we show that all three proteases can degrade unfolded model substrates, but differ with respect to cleavage sites, temperature and pH optima. For recombinant HhoA, and to a lesser extent for HtrA, we observed an interesting shift in the pH optimum from slightly acidic to alkaline in the presence of Mg2+ and Ca2+ ions. All three proteases formed different homo-oligomeric complexes with and without substrate, implying mechanistic differences in comparison with each other and with the well-studied Escherichia coli orthologues DegP (degradation of periplasmic proteins P) and DegS. Deletion of the PDZ domain decreased, but did not abolish, the proteolytic activity of all three proteases, and prevented substrate-induced formation of complexes higher than trimers by HtrA and HhoA. In summary, biochemical characterization of HtrA, HhoA and HhoB lays the foundation for a better understanding of their overlapping, but not completely redundant, stress-resistance functions in Synechocystis sp. PCC 6803.

Preliminary characterization of a photo-tolerant mutant of Synechocystis sp. PCC 6803 obtained by in vitro random mutagenesis of psbA2

Plant Science ◽  
1996 ◽  
Vol 115 (2) ◽  
pp. 261-266 ◽  
Author(s):  
Yoshihiro Narusaka ◽  
Akio Murakami ◽  
Mari Saeki ◽  
Hirokazu Kobayashi ◽  
Kimiyuki Satoh
Keyword(s):  
Random Mutagenesis ◽  
Preliminary Characterization ◽  
Tolerant Mutant ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals Characterization of Chlamydomonas reinhardtii phosphatidylglycerophosphate synthase in Synechocystis sp. PCC 6803

2015 ◽  
Vol 6 ◽  
Author(s):  
Chun-Hsien Hung ◽  
Kaichiro Endo ◽  
Koichi Kobayashi ◽  
Yuki Nakamura ◽  
Hajime Wada
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Synechocystis Sp ◽  
Pcc 6803
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