Scientific Article
previous document  unige:11107  next document
add to browser collection
Title

Phalloidin binding and rheological differences among actin isoforms

Authors
Allen, P. G.
Shuster, C. B.
Kas, J.
Janmey, P. A.
Herman, I. M.
Published in Biochemistry. 1996, vol. 35, no. 45, p. 14062-14069
Abstract Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheologic properties of purified actin isoforms from a variety of eukaryotic sources. We observe differences in the phalloidin association kinetics between muscle alpha- and cytoplasmic actins. Phalloidin dissociates from all mammalian actin isoforms tested at the same slow rate, while dissociation from yeast actin is 1 order of magnitude more rapid. The actin isoforms form viscoelastic gels to varying degrees with skeletal muscle alpha-actin gels being the most elastic, smooth muscle alpha- and gamma-actins being less elastic, and beta-actin not forming elastic structures under our experimental conditions. The sequence variation among isoforms is discussed in light of these biophysical and biochemical differences.
Keywords Actins/ chemistryAnimalsCattleCell-Free SystemChickensElasticityKineticsModels, MolecularMuscle, Skeletal/chemistryMuscle, Smooth/chemistryPhalloidine/ chemistryProtein Structure, TertiaryRabbitsRheologySaccharomyces cerevisiaeStructure-Activity RelationshipViscosity
Identifiers
PMID: 8916891
Full text
Article - document accessible for UNIGE members only Limited access to UNIGE
Other version: http://pubs.acs.org/doi/pdf/10.1021/bi961326g
Citation
(ISO format)
ALLEN, P. G. et al. Phalloidin binding and rheological differences among actin isoforms. In: Biochemistry, 1996, vol. 35, n° 45, p. 14062-14069. https://archive-ouverte.unige.ch/unige:11107

180 hits

0 download

Update

Deposited on : 2010-08-27

Export document
Format :
Citation style :