Linked Life Data

3233215

Source:http://linkedlifedata.com/resource/pubmed/id/3233215

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1989-5-1
pubmed:abstractText
Previous experiments demonstrated that two thiols of skeletal myosin subfragment 1 (SF1) could be oxidized to a disulfide bond by treatment with a 2-fold excess of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) in the presence of MgADP [Wells, J. A., & Yount, R. G. (1980) Biochemistry 19, 1711-1717]. The resulting characteristic changes in the ATPase activities of SF1 and the fact that MgADP was stably trapped at the active site [Wells, J. A., & Yount, R. G. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 4966-4970] suggested that the two thiols cross-linked were SH1 (Cys-707) and SH2 (Cys-697) from the myosin heavy chain. To verify this suggestion, SF1, after DTNB treatment as above, was treated with an excess of N-ethylmaleimide to block all accessible thiols. The single protein disulfide produced by DTNB oxidation was reduced with dithioerythritol and the modified SF1 internally cross-linked with equimolar [14C]p-phenylenedimaleimide (pPDM) in the presence of MgADP. After extensive trypsinization, the major 14C-labeled peptide was isolated, characterized, and shown to be Cys-Asn-Gly-Val-Leu-Gly-Ile-Arg-Ile-Cys-Arg, in which the two cysteines were cross-linked by pPDM. This peptide is known to contain SH2 and SH1 in this order and to come from residues 697-708 in the rabbit skeletal myosin heavy chain [Elzinga, M., & Collins, J. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 4281-4284; M. Elzinga, personal communication].(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8945-52
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:3233215-Amino Acid Sequence, pubmed-meshheading:3233215-Animals, pubmed-meshheading:3233215-Binding Sites, pubmed-meshheading:3233215-Chemical Phenomena, pubmed-meshheading:3233215-Chemistry, pubmed-meshheading:3233215-Chromatography, High Pressure Liquid, pubmed-meshheading:3233215-Cross-Linking Reagents, pubmed-meshheading:3233215-Disulfides, pubmed-meshheading:3233215-Dithionitrobenzoic Acid, pubmed-meshheading:3233215-Ethylmaleimide, pubmed-meshheading:3233215-Maleimides, pubmed-meshheading:3233215-Molecular Sequence Data, pubmed-meshheading:3233215-Myosins, pubmed-meshheading:3233215-Nucleotides, pubmed-meshheading:3233215-Oxidation-Reduction, pubmed-meshheading:3233215-Peptide Fragments, pubmed-meshheading:3233215-Protein Conformation, pubmed-meshheading:3233215-Rabbits, pubmed-meshheading:3233215-Sulfhydryl Compounds, pubmed-meshheading:3233215-Trypsin
pubmed:year
1988
pubmed:articleTitle
Flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10 A under the influence of nucleotide binding.
pubmed:affiliation
Institute of Biological Chemistry, Washington State University, Pullman 99164.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't