A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum
A full-length cDNA coding a calmodulin (CaM)-dependent protein kinase gene was cloned from Physarum plasmodia poly(A)-RNA by polymerase chain reaction with the oligonucleotide primers that were designed after the amino acid sequence of highly conserved regions of myosin light-chain kinase. Sequence...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2005-03, Vol.328 (4), p.838-844 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Nakamura, Akio Hanyuda, Yuki Okagaki, Tuyoshi Takagi, Takashi Kohama, Kazuhiro |
| description | A full-length cDNA coding a calmodulin (CaM)-dependent protein kinase gene was cloned from
Physarum plasmodia poly(A)-RNA by polymerase chain reaction with the oligonucleotide primers that were designed after the amino acid sequence of highly conserved regions of myosin light-chain kinase. Sequence analysis of the cDNA revealed that this
Physarum kinase was a 42,519-Da protein with an ATP-binding domain, Ser/Thr kinase active site signature, and CaM-binding domain. Expression of the cDNA in
Escherichia coli demonstrated that the
Physarum kinase in the presence of Ca
2+ and CaM phosphorylated the recombinant phosphorylatable light chain (PLc) of
Physarum myosin II. The peptide analysis after proteolysis of the phosphorylated PLc indicated that Ser 18 was phosphorylated. The site was confirmed by the failure of phosphorylation of PLc, the Ser 18 of which was replaced by Ala. The physiological role of the kinase will be discussed with special reference to the 55-kDa kinase, which had been previously purified from
Physarum plasmodia for phosphorylated PLc. |
| doi_str_mv | 10.1016/j.bbrc.2005.01.035 |
| format | Article |
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Physarum plasmodia poly(A)-RNA by polymerase chain reaction with the oligonucleotide primers that were designed after the amino acid sequence of highly conserved regions of myosin light-chain kinase. Sequence analysis of the cDNA revealed that this
Physarum kinase was a 42,519-Da protein with an ATP-binding domain, Ser/Thr kinase active site signature, and CaM-binding domain. Expression of the cDNA in
Escherichia coli demonstrated that the
Physarum kinase in the presence of Ca
2+ and CaM phosphorylated the recombinant phosphorylatable light chain (PLc) of
Physarum myosin II. The peptide analysis after proteolysis of the phosphorylated PLc indicated that Ser 18 was phosphorylated. The site was confirmed by the failure of phosphorylation of PLc, the Ser 18 of which was replaced by Ala. The physiological role of the kinase will be discussed with special reference to the 55-kDa kinase, which had been previously purified from
Physarum plasmodia for phosphorylated PLc.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.01.035</identifier><identifier>PMID: 15707955</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases - chemistry ; Calcium-Calmodulin-Dependent Protein Kinases - genetics ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Calmodulin-dependent protein kinase ; Cells, Cultured ; Conserved Sequence ; Escherichia coli ; Molecular Sequence Data ; Molecular Weight ; Myosin light chain ; Phosphorylation ; Physarum plasmodium ; Physarum polycephalum ; Physarum polycephalum - enzymology ; Physarum polycephalum - genetics ; Protein Binding ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Structure-Activity Relationship</subject><ispartof>Biochemical and biophysical research communications, 2005-03, Vol.328 (4), p.838-844</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-2de54965e992132cfa9894e0758a76605b111b5940e57a521d56e2b72a2a24cf3</citedby><cites>FETCH-LOGICAL-c385t-2de54965e992132cfa9894e0758a76605b111b5940e57a521d56e2b72a2a24cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2005.01.035$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15707955$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakamura, Akio</creatorcontrib><creatorcontrib>Hanyuda, Yuki</creatorcontrib><creatorcontrib>Okagaki, Tuyoshi</creatorcontrib><creatorcontrib>Takagi, Takashi</creatorcontrib><creatorcontrib>Kohama, Kazuhiro</creatorcontrib><title>A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A full-length cDNA coding a calmodulin (CaM)-dependent protein kinase gene was cloned from
Physarum plasmodia poly(A)-RNA by polymerase chain reaction with the oligonucleotide primers that were designed after the amino acid sequence of highly conserved regions of myosin light-chain kinase. Sequence analysis of the cDNA revealed that this
Physarum kinase was a 42,519-Da protein with an ATP-binding domain, Ser/Thr kinase active site signature, and CaM-binding domain. Expression of the cDNA in
Escherichia coli demonstrated that the
Physarum kinase in the presence of Ca
2+ and CaM phosphorylated the recombinant phosphorylatable light chain (PLc) of
Physarum myosin II. The peptide analysis after proteolysis of the phosphorylated PLc indicated that Ser 18 was phosphorylated. The site was confirmed by the failure of phosphorylation of PLc, the Ser 18 of which was replaced by Ala. The physiological role of the kinase will be discussed with special reference to the 55-kDa kinase, which had been previously purified from
Physarum plasmodia for phosphorylated PLc.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - chemistry</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - genetics</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Calmodulin-dependent protein kinase</subject><subject>Cells, Cultured</subject><subject>Conserved Sequence</subject><subject>Escherichia coli</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Myosin light chain</subject><subject>Phosphorylation</subject><subject>Physarum plasmodium</subject><subject>Physarum polycephalum</subject><subject>Physarum polycephalum - enzymology</subject><subject>Physarum polycephalum - genetics</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LJDEQhsPiso4ff8CD9Mlbt1XpTmcCXobBXQVBD7uwt5BOV2PG_jLpVubfm2EGvCl1qEM99VL1MHaBkCFgeb3JqsrbjAOIDDCDXPxgCwQFKUcojtgCAMqUK_x_zE5C2AAgFqX6xY5RSJBKiAV7WiXWtN1Qz63r05pG6mvqp2T0w0SuT15cbwIljR-6pB3eySc0vxi_jdPk6XkbjJ-7ZBzaraXx2bRzd8Z-NqYNdH7op-zf79u_67v04fHP_Xr1kNp8KaaU1yQKVQpSimPObWPUUhUEUiyNLEsQFSJWQhVAQhrBsRYl8UpyE6uwTX7Krva58dLXmcKkOxcsta3paZiDLmXBC8nltyDKZY4oIIJ8D1o_hOCp0aN3XfxVI-idcL3RO-F6J1wD6ig8Ll0e0ueqo_pz5WA4Ajd7gKKMN0deB-uot1Q7T3bS9eC-yv8AcV2RdQ</recordid><startdate>20050325</startdate><enddate>20050325</enddate><creator>Nakamura, Akio</creator><creator>Hanyuda, Yuki</creator><creator>Okagaki, Tuyoshi</creator><creator>Takagi, Takashi</creator><creator>Kohama, Kazuhiro</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050325</creationdate><title>A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum</title><author>Nakamura, Akio ; Hanyuda, Yuki ; Okagaki, Tuyoshi ; Takagi, Takashi ; Kohama, Kazuhiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-2de54965e992132cfa9894e0758a76605b111b5940e57a521d56e2b72a2a24cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - chemistry</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - genetics</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Calmodulin-dependent protein kinase</topic><topic>Cells, Cultured</topic><topic>Conserved Sequence</topic><topic>Escherichia coli</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Myosin light chain</topic><topic>Phosphorylation</topic><topic>Physarum plasmodium</topic><topic>Physarum polycephalum</topic><topic>Physarum polycephalum - enzymology</topic><topic>Physarum polycephalum - genetics</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakamura, Akio</creatorcontrib><creatorcontrib>Hanyuda, Yuki</creatorcontrib><creatorcontrib>Okagaki, Tuyoshi</creatorcontrib><creatorcontrib>Takagi, Takashi</creatorcontrib><creatorcontrib>Kohama, Kazuhiro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakamura, Akio</au><au>Hanyuda, Yuki</au><au>Okagaki, Tuyoshi</au><au>Takagi, Takashi</au><au>Kohama, Kazuhiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2005-03-25</date><risdate>2005</risdate><volume>328</volume><issue>4</issue><spage>838</spage><epage>844</epage><pages>838-844</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>A full-length cDNA coding a calmodulin (CaM)-dependent protein kinase gene was cloned from
Physarum plasmodia poly(A)-RNA by polymerase chain reaction with the oligonucleotide primers that were designed after the amino acid sequence of highly conserved regions of myosin light-chain kinase. Sequence analysis of the cDNA revealed that this
Physarum kinase was a 42,519-Da protein with an ATP-binding domain, Ser/Thr kinase active site signature, and CaM-binding domain. Expression of the cDNA in
Escherichia coli demonstrated that the
Physarum kinase in the presence of Ca
2+ and CaM phosphorylated the recombinant phosphorylatable light chain (PLc) of
Physarum myosin II. The peptide analysis after proteolysis of the phosphorylated PLc indicated that Ser 18 was phosphorylated. The site was confirmed by the failure of phosphorylation of PLc, the Ser 18 of which was replaced by Ala. The physiological role of the kinase will be discussed with special reference to the 55-kDa kinase, which had been previously purified from
Physarum plasmodia for phosphorylated PLc.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15707955</pmid><doi>10.1016/j.bbrc.2005.01.035</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Binding Sites Calcium-Calmodulin-Dependent Protein Kinases - chemistry Calcium-Calmodulin-Dependent Protein Kinases - genetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calmodulin-dependent protein kinase Cells, Cultured Conserved Sequence Escherichia coli Molecular Sequence Data Molecular Weight Myosin light chain Phosphorylation Physarum plasmodium Physarum polycephalum Physarum polycephalum - enzymology Physarum polycephalum - genetics Protein Binding Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Analysis, Protein Sequence Homology, Amino Acid Structure-Activity Relationship |
| title | A calmodulin-dependent protein kinase from lower eukaryote Physarum polycephalum |
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