| pubmed-article:3032987 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0027120 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0027096 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0067062 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0012120 | lld:lifeskim |
| pubmed-article:3032987 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3032987 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:3032987 | pubmed:dateCreated | 1987-6-5 | lld:pubmed |
| pubmed-article:3032987 | pubmed:abstractText | We have partially purified myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) from Dictyostelium discoideum. MLCK was purified 4,700-fold with a yield of approximately 1 mg from 350 g of cells. The enzyme is very acidic as suggested by its tight binding to DEAE. Dictyostelium MLCK has an apparent native molecular mass on HPLC G3000SW of approximately 30,000 D. Mg2+ is required for enzyme activity. Ca2+ inhibits activity and this inhibition is not relieved by calmodulin. cAMP or cGMP have no effect on enzyme activity. Dictyostelium MLCK is very specific for the 18,000-D light chain of Dictyostelium myosin and does not phosphorylate the light chain of several other myosins tested. Myosin purified from log-phase amebas of Dictyostelium has approximately 0.3 mol Pi/mol 18,000-D light chain as assayed by glycerol-urea gel electrophoresis. Dictyostelium MLCK can phosphorylate this myosin to a stoichiometry approaching 1 mol Pi/mol 18,000-D light chain. MLCP, which was partially purified, selectively removes phosphate from the 18,000-D light chain but not from the heavy chain of Dictyostelium myosin. Phosphatase-treated Dictyostelium myosin has less than or equal to 0.01 mol Pi/mol 18,000-D light chain. Phosphatase-treated myosin could be rephosphorylated to greater than or equal to 0.96 mol Pi/mol 18,000-D light chain by incubation with MLCK and ATP. We found myosin thick filament assembly to be independent of the extent of 18,000-D light-chain phosphorylation when measured as a function of ionic strength. However, actin-activated Mg2+-ATPase activity of Dictyostelium myosin was found to be directly related to the extent of phosphorylation of the 18,000-D light chain. MLCK-treated myosin moved in an in vitro motility assay (Sheetz, M. P., and J. A. Spudich, 1983, Nature (Lond.), 305:31-35) at approximately 1.4 micron/s whereas phosphatase-treated myosin moved only slowly or not at all. The effects of phosphatase treatment on the movement were fully reversed by subsequent treatment with MLCK. | lld:pubmed |
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| pubmed-article:3032987 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3032987 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3032987 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3032987 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3032987 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3032987 | pubmed:month | May | lld:pubmed |
| pubmed-article:3032987 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:3032987 | pubmed:author | pubmed-author:SpudichJ AJA | lld:pubmed |
| pubmed-article:3032987 | pubmed:author | pubmed-author:GriffithL MLM | lld:pubmed |
| pubmed-article:3032987 | pubmed:author | pubmed-author:DownsS MSM | lld:pubmed |
