Domain interactions on the ntr signal transduction pathway: two-hybrid analysis of mutant and truncated derivatives of Histidine kinase NtrB

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Title: Domain interactions on the ntr signal transduction pathway: two-hybrid analysis of mutant and truncated derivatives of Histidine kinase NtrB
Authors: Martínez Argudo, Isabel | Salinas, Paloma | Maldonado, Rafael | Contreras, Asunción
Research Group/s: Transducción de Señales en Bacterias
Center, Department or Service: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología
Keywords: Nitrogen | Two-hybrid | Transcription | Escherichia coli
Knowledge Area: Genética
Issue Date: Jan-2002
Publisher: American Society for Microbiology
Citation: MARTÍNEZ ARGUDO, Isabel, et al. “Domain interactions on the ntr signal transduction pathway: two-hybrid analysis of mutant and truncated derivatives of Histidine kinase NtrB”. Journal of Bacteriology. Vol. 184, No. 1 (Jan. 2002). ISSN 0021-9193, pp. 200-206
Abstract: We have used the yeast two-hybrid system to analyze protein-protein interactions mediated by domains of regulatory proteins of the ntr signal transduction system, including interactions among NtrB derivatives and their interactions with NtrC and PII from Klebsiella pneumoniae. Interactions took place only between proteins or protein domains belonging to the ntr signal transduction system and not between proteins or domains from noncognate regulators. NtrB and its transmitter domain, but not NtrC, CheA, or the cytoplasmic C terminus of EnvZ, interacted with PII. In addition, interaction of NtrB with NtrC, but not with PII, depended on the histidine phosphotransfer domain. Point mutation A129T, diminishing the NtrC phosphatase activity of NtrB, affected the strength of the signals between NtrC and the transmitter module of NtrB but had no impact on PII signals, suggesting that A129T prevents the conformational change needed by NtrB to function as a phosphatase for NtrC, rather than disturbing binding to PII.
Sponsor: This work was supported by grant PB97-0115 from the Ministerio de Educación y Cultura.
URI: http://hdl.handle.net/10045/1729
ISSN: 0021-9193
DOI: 10.1128/JB.184.1.200-206.2002
Language: eng
Type: info:eu-repo/semantics/article
Peer Review: si
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