Identification and analysis of Escherichia coli proteins that interact with the histidine kinase NtrB in a yeast two-hybrid system

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Title: Identification and analysis of Escherichia coli proteins that interact with the histidine kinase NtrB in a yeast two-hybrid system
Authors: Salinas, Paloma | Contreras, Asunción
Research Group/s: Transducción de Señales en Bacterias
Center, Department or Service: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología
Keywords: Escherichia coli | Two-hybrid | Protein interaction | Nitrogen regulation | NtrB | GlnK | Aspartase | Nitrogen interaction network
Knowledge Area: Genética
Issue Date: 28-Jun-2003
Publisher: Springer
Citation: SALINAS BERNÁ, Paloma; CONTRERAS DE VERA, Asunción. “Identification and analysis of Escherichia coli proteins that interact with the histidine kinase NtrB in a yeast two-hybrid system”. Molecular Genetics and Genomics. Vol. 269, No. 4 (July 2003). ISSN 1617-4615, pp. 574-581
Abstract: In this work we used the yeast two-hybrid (Y2H) system to deepen our understanding of protein-protein interactions that are involved in the nitrogen regulatory network in Escherichia coli. Three different genes, encoding GlnB, GlnK and AspA, respectively, were found among 64 positive clones identified from E. coli Sau 3AI Y2H libraries using the nitrogen regulator NtrB as bait. Structural and functional analysis of the prey clones provided information on library features and the degree of saturation achieved in the screens. Further analysis revealed that the C-terminal kinase domain of NtrB is required for the interaction with GlnK, while AspA91–312 interacts specifically with the conserved histidine phosphotransfer domain of NtrB, thus providing additional evidence for the involvement of the conserved transmitter module of the histidine kinase NtrB in input sensory functions.
Sponsor: This work was supported by a grant (BMC2001-0863) from the Ministerio de Educación y Cultura.
URI: http://hdl.handle.net/10045/1726
ISSN: 1617-4615
DOI: 10.1007/s00438-003-0866-7
Language: eng
Type: info:eu-repo/semantics/article
Rights: The original publication is available at www.springerlink.com
Peer Review: si
Publisher version: http://dx.doi.org/10.1007/s00438-003-0866-7
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