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Title: SipA, a novel type of protein from Synechococcus sp. PCC 7942, binds to the kinase domain of NblS. Author: Espinosa J, Fuentes I, Burillo S, Rodríguez-Mateos F, Contreras A. Journal: FEMS Microbiol Lett; 2006 Jan; 254(1):41-7. PubMed ID: 16451177. Abstract: Cyanobacteria respond to nutrient stress conditions by degrading their light-harvesting complexes for photosynthesis, a process regulated in Synechococcus sp. PCC 7942 by the sensor histidine kinase non-bleaching sensor (NblS). In yeast two-hybrid screenings for proteins interacting with NblS we have identified a novel type of protein, named SipA for NblS interacting protein A. Specific binding between NblS and SipA is observed with both yeast and bacterial two-hybrid systems. Additional yeast two-hybrid screenings with SipA as bait further confirmed the specificity of the interaction and allowed us to map their determinants to the ATP-binding domain of NblS. Strong conservation and coevolution of both NblS and SipA in cyanobacteria further suggests the importance of SipA in the context of the NblS signal transduction network.[Abstract] [Full Text] [Related] [New Search]