Espinosa Javier, Fuentes Inmaculada, Burillo Sergio, Rodríguez-Mateos Francisco, Contreras Asunción
División de Genética, Universidad de Alicante, Alicante, Spain.
FEMS Microbiol Lett. 2006 Jan;254(1):41-7. doi: 10.1111/j.1574-6968.2005.00007.x.
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.
蓝细菌通过降解其用于光合作用的光捕获复合物来应对营养胁迫条件,这一过程在聚球藻属PCC 7942中由传感组氨酸激酶非漂白传感器(NblS)调控。在酵母双杂交筛选与NblS相互作用的蛋白质时,我们鉴定出一种新型蛋白质,命名为SipA(NblS相互作用蛋白A)。在酵母和细菌双杂交系统中均观察到NblS与SipA之间的特异性结合。以SipA为诱饵进行的额外酵母双杂交筛选进一步证实了这种相互作用的特异性,并使我们能够将它们的决定因素定位到NblS的ATP结合结构域。蓝细菌中NblS和SipA的强烈保守性和共同进化进一步表明SipA在NblS信号转导网络中的重要性。