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Title

Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases

AuthorsMiguel-Romero, Laura ; Mideros-Mora, Cristina; Marina, Alberto ; Casino, Patricia
KeywordsCis–trans autophosphorylation
Heterodimer production and purification
Histidine kinases
Signal transduction
Two-component systems
X-ray crystallography
Issue DateJan-2020
PublisherSpringer
CitationMethods in Molecular Biology 2077:121-140 (2020)
AbstractAutophosphorylation of histidine kinases (HK) is the first step for signal transduction in bacterial two-component signalling systems. As HKs dimerize, the His residue is phosphorylated in cis or trans depending on whether the ATP molecule used in the reaction is bound to the same or the neighboring subunit, respectively. The cis or trans autophosphorylation results from an alternative directionality in the connection between helices α1 and α2 in the HK DHp domain, in such a way that α2 could be oriented almost 90° counterclockwise or clockwise with respect to α1. Sequence and length variability of this connection appears to lie behind the different directionality and is implicated in partner recognition with the response regulator (RR), highlighting its importance in signal transduction. Despite this mechanistic difference, HK autophosphorylation appears to be universal, involving conserved residues neighboring the phosphoacceptor His residue. Herein, we describe a simple protocol to determine both autophosphorylation directionality of HKs and the roles of the catalytic residues in these protein kinases.
Description20 páginas, 6 figuras
Publisher version (URL)http://dx.doi.org/10.1007/978-1-4939-9884-5_9
URIhttp://hdl.handle.net/10261/209736
DOI10.1007/978-1-4939-9884-5_9
ISSN1064-3745
E-ISSN1940-6029
Appears in Collections:(IBV) Artículos
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