Volume 254, Issue 1 pp. 41-47

SipA, a novel type of protein from Synechococcus sp. PCC 7942, binds to the kinase domain of NblS

Javier Espinosa

Javier Espinosa

División de Genética, Universidad de Alicante, Alicante, Spain

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Inmaculada Fuentes

Inmaculada Fuentes

División de Genética, Universidad de Alicante, Alicante, Spain

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Sergio Burillo

Sergio Burillo

División de Genética, Universidad de Alicante, Alicante, Spain

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Francisco Rodríguez-Mateos

Francisco Rodríguez-Mateos

Departamento de Matemática Aplicada, Universidad de Alicante, Alicante, Spain

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Asunción Contreras

Asunción Contreras

División de Genética, Universidad de Alicante, Alicante, Spain

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First published: 09 November 2005
Citations: 7
Asunción Contreras, División de Genética, Facultad de Ciencias, Universidad de Alicante, Apartado 99, E-03080 Alicante, Spain. Tel.: +34 96 590 3957; fax: +34 96 590 9569; e-mail: [email protected]

Editor: Karl Forchhammer

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.

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