SipA, a novel type of protein from Synechococcus sp. PCC 7942, binds to the kinase domain of NblS.
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.
Espinosa
Javier
J
División de Genética, Universidad de Alicante, Alicante, Spain.
Fuentes
Inmaculada
I
Burillo
Sergio
S
Rodríguez-Mateos
Francisco
F
Contreras
Asunción
A
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D015964:Gene Expression Regulation, Bacterial; D018869:Heat-Shock Response; D000071677:Histidine Kinase; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D046940:Synechococcus / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D020798:Two-Hybrid System Techniques
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D000071677:Histidine Kinase