Alteration in crossbridge kinetics caused by mutations in actin

The generation of force during muscle contraction results from the interaction of myosin and actin. The kinetics of this force generation vary between different muscle types and within the same muscle type in different species. Most attention has focused on the role of myosin isoforms in determining...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1990-11, Vol.348 (6300), p.440-442
Main Authors: Drummond, D.R, Peckham, M, Sparrow, J.C, White, D.C.S
Format: Article
Language:English
Subjects:
Actin
Actins - physiology
Actins - ultrastructure
Amino acids
Animals
Binding sites
Biochemistry
Biological and medical sciences
Biology
Cellular biology
Classical genetics, quantitative genetics, hybrids
Disruption
DNA Mutational Analysis
Drosophila
Drosophila melanogaster
Electrophoresis, Gel, Two-Dimensional
Flight, Animal
Fundamental and applied biological sciences. Psychology
Genetics of eukaryotes. Biological and molecular evolution
Heterozygote
insect flight muscles
Insects
Invertebrata
Isoforms
Kinetics
Mechanical measurement
Mechanics
Medical research
Microscopy
Microscopy, Electron
Muscle Contraction
Muscles
Muscles - physiology
Muscles - ultrastructure
Muscular function
Muscular system
Mutation
Myosin
Structure-Activity Relationship
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The generation of force during muscle contraction results from the interaction of myosin and actin. The kinetics of this force generation vary between different muscle types and within the same muscle type in different species. Most attention has focused on the role of myosin isoforms in determining these differences. The role of actin isoforms has received little attention, largely because of the lack of a suitable cell type in which the myosin isoform remains constant yet the actin isoforms vary. An alternative approach would be to examine the effect of actin mutations, however, most of these cause such gross disruption of muscle structure that mechanical measurements are impossible. We have now identified two actin mutations which, despite involving conserved amino acids, can assemble into virtually normal myofibrils. These amino-acid changes in actin significantly affect the kinetics of force generation by muscle fibres. One of the mutations is not in the putative myosin-binding site, demonstrating the importance of long-range effects of amino acids on actin function.
ISSN:0028-0836
1476-4687
DOI:10.1038/348440a0