Linked Life Data

12222828

Source:http://linkedlifedata.com/resource/pubmed/id/12222828

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2002-9-11
pubmed:abstractText
The similarity of amino acid sequence and motifs of the N-terminal extensions of certain class II myosin light chains, found throughout the animal kingdom, suggest a common functional role. One possible role of the N-terminal extension is to enhance oscillatory work and power production in striated muscles that normally operate in an oscillatory mode. We conducted small-angle X-ray diffraction experiments and small-length-perturbation analysis to examine the structural and functional consequences of deleting the N-terminal extension of the myosin regulatory light chain (RLC) in Drosophila flight muscle. The in vivo lattice spacing of dorsal longitudinal muscle (DLM) of flies lacking the RLC N-terminal extension (Dmlc2delta2-46) was approximately 1 nm less than that of wild type (48.56 +/- 0.02 nm). The myofilament lattice of detergent-treated, demembranated DLM swelled, with the DmlcdeltaA2-46 lattice expanding more than wild type and requiring roughly twice the concentration of Dextran T500 to restore its lattice to in vivo spacing (9-10% vs. 4% w/v). The calcium sensitivity and maximum amplitude of net oscillatory work near the in vivo lattice spacing was significantly lower in Dmlc2delta2-46 compared to wild type (pCa50 shifted by approximately one-third of a pCa unit; amplitude reduced by approximately one-half). These changes were in contrast to the lack of effect reported in a previous study carried out in the absence of Dextran T500. The results are consistent with the N-terminal extension interacting with actin to increase the probability that crossbridges form during stretch-activated oscillatory work and power production, especially at submaximal levels of calcium activation.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0142-4319
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
675-83
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Changes in myofibrillar structure and function produced by N-terminal deletion of the regulatory light chain in Drosophila.
pubmed:affiliation
Department of Biological, Chemical and Physical Sciences, Illinois Institute of Technology, Chicago 60616, USA.
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