Research Repository

Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.

Paynter, Jennifer J and Andres-Enguix, Isabelle and Fowler, Philip W and Tottey, Stephen and Cheng, Wayland and Enkvetchakul, Decha and Bavro, Vassiliy N and Kusakabe, Yoshio and Sansom, Mark SP and Robinson, Nigel J and Nichols, Colin G and Tucker, Stephen J (2010) 'Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.' The Journal of Biological Chemistry, 285 (52). 40754 - 40761. ISSN 0021-9258

[img]
Preview
Text
Functional complementation and genetic deletion studies of KirBac channels activatory mutations highlight gating-sensitive d.pdf - Published Version
Available under License Creative Commons Attribution Non-commercial.

Download (1MB) | Preview

Abstract

The superfamily of prokaryotic inwardly rectifying (KirBac) potassium channels is homologous to mammalian Kir channels. However, relatively little is known about their regulation or about their physiological role in vivo. In this study, we have used random mutagenesis and genetic complementation in K(+)-auxotrophic Escherichia coli and Saccharomyces cerevisiae to identify activatory mutations in a range of different KirBac channels. We also show that the KirBac6.1 gene (slr5078) is necessary for normal growth of the cyanobacterium Synechocystis PCC6803. Functional analysis and molecular dynamics simulations of selected activatory mutations identified regions within the slide helix, transmembrane helices, and C terminus that function as important regulators of KirBac channel activity, as well as a region close to the selectivity filter of KirBac3.1 that may have an effect on gating. In particular, the mutations identified in TM2 favor a model of KirBac channel gating in which opening of the pore at the helix-bundle crossing plays a far more important role than has recently been proposed.

Item Type: Article
Uncontrolled Keywords: Synechocystis, Escherichia coli, Saccharomyces cerevisiae, Escherichia coli Proteins, Potassium Channels, Inwardly Rectifying, Saccharomyces cerevisiae Proteins, Genetic Complementation Test, Ion Channel Gating, Protein Structure, Secondary, Protein Structure, Tertiary, Mutation
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Elements
Date Deposited: 28 Jun 2021 10:35
Last Modified: 28 Jun 2021 11:15
URI: http://repository.essex.ac.uk/id/eprint/30225

Actions (login required)

View Item View Item