Exploration of a Possible Partnership among Orphan Two-Component System Proteins in CyanobacteriumSynechococcus elongatusPCC 7942
| Autor: | Hirofumi Yoshikawa, Taku Chibazakura, Yuzuru Tozawa, Hiroaki Kato, Satoru Watanabe, Kaori Nimura-Matsune |
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| Rok vydání: | 2012 |
| Předmět: |
Histidine Kinase
Operon Two-hybrid screening Biology Applied Microbiology and Biotechnology Biochemistry Genome Analytical Chemistry Bacterial Proteins Stress Physiological Two-Hybrid System Techniques Sasa Protein Interaction Mapping Botany Escherichia coli Cloning Molecular Phosphorylation Molecular Biology Gene Adaptor Proteins Signal Transducing Synechococcus Genetics Organic Chemistry Histidine kinase Signal transducing adaptor protein Gene Expression Regulation Bacterial General Medicine biology.organism_classification Adaptation Physiological Two-component regulatory system Protein Structure Tertiary Protein Kinases Genome Bacterial Signal Transduction Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 76:1484-1491 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.120172 |
| Popis: | To understand the induction of the adaptive response under various stress conditions, it is important to determine the partnership between histidine kinase and response regulators in the bacterial two-component system (TCS). The genes encoding TCS partners are usually comprised of an operon in the genome, but many of them are orphans in the cyanobacterial genome. There is little information on their partnerships in Synechococcus elongatus PCC 7942. Our comprehensive analysis of protein-protein interactions among all 37 full-length proteins and the truncated domains of 24 orphans revealed a number of specific interactions. They involved evolutionarily well-conserved orphan proteins among cyanobacterial species such as Synpcc7942_0453/Ycf29, NblS/RpaB, NblS/SrrA, SasA/RpaA, and SasA/Synpcc7942_2466. Our investigation of the transphosphorylation of interaction partners indicates that orphan TCSs comprise a complex signaling network. |
| Databáze: | OpenAIRE |
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