The Serine Protease HhoA from Synechocystis sp . PCC 6803 : 1 Substrate Specificity and Formation of a Hexameric Complex 2 are Regulated by the PDZ Domain 3 4 Running title : Synechocystis serine

نویسنده

  • Iwona Adamska
چکیده

4 Running title: Synechocystis serine protease HhoA 5 6 Pitter F. Huesgen, Philipp Scholz and Iwona Adamska* 7 8 Department of Physiology and Plant Biochemistry, University of Konstanz, 9 Universitätsstrasse 10, D-78457 Konstanz, Germany 10 11 12 13 14 15 16 17 18 * Corresponding author. Mailing address: Department of Physiology and Plant 19 Biochemistry, University of Konstanz, Universitätsstrasse 10, D-78457 Konstanz, 20 Germany. Phone: +49 7531 88 2561. Fax +49 7531 88 3042. E-mail: 21 [email protected]. 22 AC CE PT ED Copyright © 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.00883-07 JB Accepts, published online ahead of print on 6 July 2007

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The serine protease HhoA from Synechocystis sp. strain PCC 6803: substrate specificity and formation of a hexameric complex are regulated by the PDZ domain.

Enzymes of the ATP-independent Deg serine endopeptidase family are very flexible with regard to their substrate specificity. Some family members cleave only one substrate, while others act as general proteases on unfolded substrates. The proteolytic activity of Deg proteases is regulated by PDZ protein interaction domains. Here we characterized the HhoA protease from Synechocystis sp. strain PC...

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The Serine Protease HhoA from Synechocystis sp . PCC 6803 : 1 Substrate Specificity and Formation of a Hexameric Complex 2 are Regulated by the PDZ Domain 3 4 Running title : Synechocystis

4 Running title: Synechocystis serine protease HhoA 5 6 Pitter F. Huesgen, Philipp Scholz and Iwona Adamska* 7 8 Department of Physiology and Plant Biochemistry, University of Konstanz, 9 Universitätsstrasse 10, D-78457 Konstanz, Germany 10 11 12 13 14 15 16 17 18 * Corresponding author. Mailing address: Department of Physiology and Plant 19 Biochemistry, University of Konstanz, Universitätsstr...

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

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 ...

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Degradation of PsbO by the Deg Protease HhoA Is Thioredoxin Dependent

The widely distributed members of the Deg/HtrA protease family play an important role in the proteolysis of misfolded and damaged proteins. Here we show that the Deg protease rHhoA is able to degrade PsbO, the extrinsic protein of the Photosystem II (PSII) oxygen-evolving complex in Synechocystis sp. PCC 6803 and in spinach. PsbO is known to be stable in its oxidized form, but after reduction b...

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Metabolomic basis of laboratory evolution of butanol tolerance in photosynthetic Synechocystis sp. PCC 6803

BACKGROUND Recent efforts demonstrated the potential application of cyanobacteria as a "microbial cell factory" to produce butanol directly from CO2. However, cyanobacteria have very low tolerance to the toxic butanol, which limits the economic viability of this renewable system. RESULTS Through a long-term experimental evolution process, we achieved a 150% increase of the butanol tolerance i...

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تاریخ انتشار 2007