Linked Life Data

7844829

Source:http://linkedlifedata.com/resource/pubmed/id/7844829

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-3-3
pubmed:abstractText
A large body of biochemical evidence suggests that the F-actin filament can have internal cooperativity. We have observed large cooperative effects on the low-resolution structure of actin filaments under three very different conditions. First, when G-Ca(2+)-actin is polymerized by both Mg2+ and KCl, filaments may be found in two different populations, with two discrete positions seen for subdomain 2. When G-Ca2+ actin is polymerized by only Mg2+, a single F-Mg(2+)-actin population is seen. The structural data suggest that an entire filament exists with subdomain 2 in one state or the other when there is a heterogenous mixture of Mg2+ and Ca(2+)-actin. Second, when actin filaments are nucleated from gelsolin there is a conformational change that can be observed throughout the filament that is consistent with a large shift in the actin C terminus. There must be a large cooperative propagation of this effect throughout the filament from the nucleation point. Third, we have used phalloidin to stabilize F-actin in which two C-terminal residues have been proteolytically removed by trypsin. It has been shown biochemically that this stabilization occurs at substoichiometric amounts of phalloidin. Phalloidin, at either a 1:1 or a 1:20 molar ratio with actin, restores the connectivity between the long-pitch helical strands. F-actin's internal cooperativity will have large implications in vivo, particularly in muscle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
245
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
598-607
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Structural dynamics of F-actin: II. Cooperativity in structural transitions.
pubmed:affiliation
Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis 55455.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't