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Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium

Tsiavaliaris, Georgios, Fujita-Becker, Setsuko, Batra, Renu, Levitsky, Dmitrii I., Kull, F. Jon, Geeves, Michael A., Manstein, Dietmar J. (2002) Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium. EMBO Reports, 3 (11). pp. 1099-1105. ISSN 1469-221X. (doi:10.1093/embo-reports/kvf214) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:4012)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1093/embo-reports/kvf214

Abstract

Dominant-negative inhibition is a powerful genetic tool for the characterization of gene function in vivo, based on the specific impairment of a gene product by the coexpression of a mutant version of the same gene product. We describe the detailed characterization of two myosin constructs containing either point mutations F487A or F506G in the relay region. Dictyostelium cells transformed with F487A or F506G myosin are unable to undergo processes that require myosin II function, including fruiting-body formation, normal cytokinesis and growth in suspension. Our results show that the dominant-negative inhibition of myosin function is caused by disruption of the communication between active site and lever arm, which blocks motor activity completely, and perturbation of the communication between active site and actin-binding site, leading to an approximately 100-fold increase in the mutants' affinity for actin in the presence of ATP.

Item Type: Article
DOI/Identification number: 10.1093/embo-reports/kvf214
Additional information: 1469-221X (Print) Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Actins/metabolism Animals Calorimetry, Differential Scanning Cell Division/physiology Dictyostelium/cytology/genetics/*physiology Ligands Models, Molecular Molecular Motor Proteins *Mutation Myosin Type II/chemistry/*genetics/*metabolism Protein Conformation Protein Structure, Tertiary
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Michael Geeves
Date Deposited: 04 Sep 2008 15:54 UTC
Last Modified: 16 Nov 2021 09:42 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/4012 (The current URI for this page, for reference purposes)

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