Linked Life Data

6610679

Source:http://linkedlifedata.com/resource/pubmed/id/6610679

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1984-8-20
pubmed:abstractText
Stoichiometric amounts of MgATP disassemble dephosphorylated smooth muscle and nonmuscle myosin filaments to a 10 S monomer. Phosphorylation of the regulatory light chain reassembles the myosin into filaments (Suzuki, H., Onishi, H., Takahashi, K., and Watanabe, S. (1978) J. Biochem. (Tokyo) 84, 1529-1542). The conformation of the dephosphorylated 10 S monomer is highly unusual in that the 1500 A long myosin tail is folded into approximately equal thirds (Onishi, H., and Wakabayashi, T. (1982) J. Biochem. (Tokyo) 92, 871-879; Trybus, K. M., Huiatt, T. W., and Lowey, S. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 6151-6155). It was recently reported that phosphorylation of the regulatory light chain causes the bent monomer to unfold to the extended conformation characteristic of 6 S myosin in high salt (Craig, R., Smith, R., and Kendrick-Jones, J. (1983) Nature (Lond.) 302, 436-439). Here we show that phosphorylated myosin can exist in a stable 10 S conformation provided that the salt concentration is kept sufficiently low. Only in a narrow range of salt concentration does the monomer conformation depend on the state of phosphorylation. Above 0.3 M KCl, all myosins revert to the extended form; below 0.1 M KCl, all monomeric myosin is folded. As the salt concentration is decreased to 0.05 M KCl, the 10 S monomers form antiparallel folded dimers. Because phosphorylation increases filament formation even when 10 S monomer remains in equilibrium with polymer, assembly could proceed via the association of 10 S monomers or by a transient 6 S intermediate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8564-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't