Protein phosphatases and protein kinases in dictyostelium

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dc.contributor.authorFerris, Douglas K.en
dc.contributor.committeechairRutherford, Charles L.en
dc.contributor.committeememberMcNabb, F. Anneen
dc.contributor.committeememberYousten, Allan A.en
dc.contributor.committeememberClaus, George W.en
dc.contributor.committeememberGregory, Eugene "Mick"en
dc.contributor.departmentBiologyen
dc.date.accessioned2014-08-13T14:39:02Zen
dc.date.available2014-08-13T14:39:02Zen
dc.date.issued1986en
dc.description.abstractIn the present work, the chromatographic behavior and partial characterization of 5 protein phosphatases, 6 paranitrophenyl phosphate (pnpp) phosphatases and 2 protein kinases from <i>Dictyostelium</i> are described. .Two of the protein phosphatases are shown to have subunit structures. All of the protein phosphatase activities described were able to dephosphorylate sites on proteins that had previously been phosphorylated by the cAMP-dependent protein kinase. Therefore it may be that these phosphatases function <i>in vivo</i> to antagonize the action of the cAMP-dependent protein kinase. Various pnpp phosphatase activities, varying in size, cation requirements and pH optima are described. Since many pnpp phosphatases also function with protein substrates it is possible that these activities represent protein phosphatases that function with phosphoproteins that have not been tested. Evidence for the existence of protein kinase C in Dictyostelium is presented. A histone protein kinase was found in <i>Dictyostelium</i> extracts that eluted from DE52 cellulose at the same salt concentration that rabbit brain protein kinase C did. In addition in one experiment clear dependency on calcium and phospholipids is shown. The purification to homogeneity, and characterization of a low molecular weight autophosphorylating protein kinase, pp20, is described. This protein kinase is a major phosphorylated protein and in addition represents at least 0.03% of the total cellular protein. The autophosphorylation reaction can be inhibited by EDTA but not by EGTA. Following inhibition by EDTA, autophosphorylation can be reactivated by the addition of Mn²⁺, Mg²⁺, or Ca²⁺. Western blotting evidence is presented that shows cross reactivity of pp20 and an 85 KDa protein that may possess casein kinase activity.en
dc.description.adminincomplete_metadataen
dc.description.degreePh. D.en
dc.format.extentxi, 122 leavesen
dc.format.mimetypeapplication/pdfen
dc.identifier.urihttp://hdl.handle.net/10919/50017en
dc.publisherVirginia Polytechnic Institute and State Universityen
dc.relation.isformatofOCLC# 15295020en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subject.lccLD5655.V856 1986.F477en
dc.subject.lcshCells -- Growthen
dc.subject.lcshProteins -- Synthesisen
dc.titleProtein phosphatases and protein kinases in dictyosteliumen
dc.typeDissertationen
dc.type.dcmitypeTexten
thesis.degree.disciplineBiologyen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.leveldoctoralen
thesis.degree.namePh. D.en

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