Integrated proteomic and metabolomic characterization of a novel two-component response regulator Slr1909 involved in acid tolerance in Synechocystis sp. PCC 6803

2014 ◽  
Vol 109 ◽  
pp. 76-89 ◽  
Author(s):  
Qiang Ren ◽  
Mengliang Shi ◽  
Lei Chen ◽  
Jiangxin Wang ◽  
Weiwen Zhang
Keyword(s):  
Response Regulator ◽  
Acid Tolerance ◽  
Two Component ◽  
Synechocystis Sp ◽  
Pcc 6803

An orphan two-component response regulator Slr1588 involves salt tolerance by directly regulating synthesis of compatible solutes in photosynthetic Synechocystis sp. PCC 6803

2014 ◽  
Vol 10 (7) ◽  
pp. 1765-1774 ◽  
Author(s):  
Lei Chen ◽  
Lina Wu ◽  
Ye Zhu ◽  
Zhongdi Song ◽  
Jiangxin Wang ◽  
...  
Keyword(s):  
Salt Stress ◽  
Salt Tolerance ◽  
Response Regulator ◽  
Compatible Solutes ◽  
Two Component ◽  
Synechocystis Sp ◽  
Pcc 6803

We report here the characterization of a novel orphan response regulator Slr1588 directly involved in the synthesis and transport of compatible solutes against salt stress.

scholarly journals Physiological and Molecular Characterization of a Synechocystis sp. PCC 6803 Mutant Lacking Histidine Kinase Slr1759 and Response Regulator Slr1760

2006 ◽  
Vol 61 (11-12) ◽  
pp. 865-878 ◽  
Author(s):  
Anke Nodop ◽  
Iwane Suzuki ◽  
Aiko Barsch ◽  
Ann-Kristin Schröder ◽  
Karsten Niehaus ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Ph Value ◽  
Response Regulator ◽  
Two Component System ◽  
Component System ◽  
Bg11 Medium ◽  
Two Component ◽  
Metabolic Activities ◽  
Synechocystis Sp ◽  
Pcc 6803

Abstract The hybrid sensory histidine kinase Slr1759 of the cyanobacterium Synechocystis sp. strain PCC 6803 contains multiple sensory domains and a multi-step phosphorelay system. Immuno blot analysis provided evidence that the histidine kinase Slr1759 is associated with the cytoplasmic membrane. The gene slr1759 is part of an operon together with slr1760, encoding a response regulator. A comparative investigation was performed on Synechocystis sp. strain PCC 6803 wild type (WT) and an insertionally inactivated slr1759-mutant (Hik14) which also lacks the transcript for the response regulator Slr1760. The mutant Hik14 grew significantly slower than WT in the early growth phase, when both were inoculated with a low cell density into BG11 medium without additional buffer and when aerated with air enriched with 2% CO2. Since the aeration with CO2-enriched air results in a decrease of the pH value in the medium, the growth experiments indicated that Hik14 is not able to adjust its metabolic activities as rapidly as WT to compensate for a larger decrease of the pH value in the medium. No significant differences in growth between Hik14 and WT were observed when cells were inoculated with a higher cell density in BG11 medium or when the BG11 medium contained 50 mm Epps-NaOH, pH 7.5, to prevent the pH drop. This Hik14 phenotype has so far only been seen under the above defined growth condition. Results of photosynthetic activity measurements as well as Northern blot-, immuno blot-, and metabolite analyses suggest that the two-component system Slr1759/Slr1760 has a function in the coordination of several metabolic activities which is in good agreement with the complex domain structure of Slr1759. The direct targets of this two-component system have so far not been identified.

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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