Role of Essential Light Chain EF Hand Domains in Calcium Binding and Regulation of Scallop Myosin
The specific Ca2+binding site that triggers contraction of molluscan muscle requires the presence of an essential light chain (ELC) from a Ca2+binding myosin. Of the four EF hand-like domains in molluscan ELCs, only domain III has an amino acid sequence predicted to be capable of binding Ca2+. In th...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-08, Vol.92 (17), p.7652-7656 |
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| creator | Fromherz, Sylvia Szent-Gyorgyi, Andrew G. |
| description | The specific Ca2+binding site that triggers contraction of molluscan muscle requires the presence of an essential light chain (ELC) from a Ca2+binding myosin. Of the four EF hand-like domains in molluscan ELCs, only domain III has an amino acid sequence predicted to be capable of binding Ca2+. In this report, we have used mutant ELCs to locate the Ca2+binding site in scallop myosin and to probe the role of the ELC in regulation. Point mutations in domain III of scallop ELC have no effect on Ca2+binding. Interestingly, scallop and rat cardiac ELC chimeras support Ca2+binding only if domain I is scallop. These results are nevertheless in agreement with structural studies on a proteolytic fragment of scallop myosin, the regulatory domain. Furthermore, Ca2+sensitivity of the scallop myosin ATPase requires scallop ELC domain I: ELCs containing cardiac domain I convert scallop myosin to an unregulated molecule whose activity is no longer repressed in the absence of Ca2+. Despite its unusual EF hand domain sequence, our data indicate that the unique and required contribution of molluscan ELCs to Ca2+binding and regulation of molluscan myosins resides exclusively in domain I. |
| doi_str_mv | 10.1073/pnas.92.17.7652 |
| format | Article |
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Of the four EF hand-like domains in molluscan ELCs, only domain III has an amino acid sequence predicted to be capable of binding Ca2+. In this report, we have used mutant ELCs to locate the Ca2+binding site in scallop myosin and to probe the role of the ELC in regulation. Point mutations in domain III of scallop ELC have no effect on Ca2+binding. Interestingly, scallop and rat cardiac ELC chimeras support Ca2+binding only if domain I is scallop. These results are nevertheless in agreement with structural studies on a proteolytic fragment of scallop myosin, the regulatory domain. Furthermore, Ca2+sensitivity of the scallop myosin ATPase requires scallop ELC domain I: ELCs containing cardiac domain I convert scallop myosin to an unregulated molecule whose activity is no longer repressed in the absence of Ca2+. Despite its unusual EF hand domain sequence, our data indicate that the unique and required contribution of molluscan ELCs to Ca2+binding and regulation of molluscan myosins resides exclusively in domain I.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.17.7652</identifier><identifier>PMID: 7644472</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenosine triphosphatases ; Amino Acid Sequence ; Amino acids ; Animals ; Binding Sites ; Biochemistry ; Calcium ; Calcium - metabolism ; Chimeras ; Cloning, Molecular ; Consensus Sequence ; Divalent cations ; Gels ; Homeostasis ; Hybridity ; Marine ; Molecular Sequence Data ; Mollusca ; Mollusks ; Muscular system ; Mutagenesis, Site-Directed ; Mutation ; Myocardium - metabolism ; Myosins - biosynthesis ; Myosins - chemistry ; Myosins - metabolism ; Pectinidae ; Physiological regulation ; Polymerase Chain Reaction ; Protein Binding ; Proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Scallops ; Sequence Homology, Amino Acid</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-08, Vol.92 (17), p.7652-7656</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Aug 15, 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c586t-aa20d4758a3a6a665fa07158d42fdfa9c203d1ef3363afc2cf8c70a07e18ed53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/17.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2368106$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2368106$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7644472$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fromherz, Sylvia</creatorcontrib><creatorcontrib>Szent-Gyorgyi, Andrew G.</creatorcontrib><title>Role of Essential Light Chain EF Hand Domains in Calcium Binding and Regulation of Scallop Myosin</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The specific Ca2+binding site that triggers contraction of molluscan muscle requires the presence of an essential light chain (ELC) from a Ca2+binding myosin. Of the four EF hand-like domains in molluscan ELCs, only domain III has an amino acid sequence predicted to be capable of binding Ca2+. In this report, we have used mutant ELCs to locate the Ca2+binding site in scallop myosin and to probe the role of the ELC in regulation. Point mutations in domain III of scallop ELC have no effect on Ca2+binding. Interestingly, scallop and rat cardiac ELC chimeras support Ca2+binding only if domain I is scallop. These results are nevertheless in agreement with structural studies on a proteolytic fragment of scallop myosin, the regulatory domain. Furthermore, Ca2+sensitivity of the scallop myosin ATPase requires scallop ELC domain I: ELCs containing cardiac domain I convert scallop myosin to an unregulated molecule whose activity is no longer repressed in the absence of Ca2+. Despite its unusual EF hand domain sequence, our data indicate that the unique and required contribution of molluscan ELCs to Ca2+binding and regulation of molluscan myosins resides exclusively in domain I.</description><subject>Adenosine triphosphatases</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Calcium</subject><subject>Calcium - metabolism</subject><subject>Chimeras</subject><subject>Cloning, Molecular</subject><subject>Consensus Sequence</subject><subject>Divalent cations</subject><subject>Gels</subject><subject>Homeostasis</subject><subject>Hybridity</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Mollusca</subject><subject>Mollusks</subject><subject>Muscular system</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Myocardium - metabolism</subject><subject>Myosins - biosynthesis</subject><subject>Myosins - chemistry</subject><subject>Myosins - metabolism</subject><subject>Pectinidae</subject><subject>Physiological regulation</subject><subject>Polymerase Chain Reaction</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Scallops</subject><subject>Sequence Homology, Amino Acid</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2P0zAUxC0EWkrhzAWQxQFO6fordiJxgdJlkYqQlr1bD8duXbl2iRPE_vc4aqlYDpwse34zfk-D0HNKFpQofnmIkBctW1C1ULJmD9CMkpZWUrTkIZoRwlTVCCYeoyc57wghbd2QC3ShpBBCsRmCmxQsTg6vcrZx8BDw2m-2A15uwUe8usLXEDv8Me3LNePytIRg_LjHH3zsfNzgSb6xmzHA4FOcor4ZCCEd8Je7lH18ih45CNk-O51zdHu1ul1eV-uvnz4v368rUzdyqAAY6YSqG-AgQcraAVG0bjrBXOegNYzwjlrHueTgDDOuMYoUxtLGdjWfo3fH2MP4fW87U5bpIehD7_fQ3-kEXt9Xot_qTfqpBS3Jxf7mZO_Tj9HmQe99NjYEiDaNWVPZqFaUv-fo9T_gLo19LJtpRihruRDTMJdHyPQp59668xyU6Kk3PfWmW6ap0lNvxfHy7_HP_Kmoor866ZPxj3ov4O1_Ae3GEAb7ayjkiyO5y0PqzyjjsqFE8t-zRLXb</recordid><startdate>19950815</startdate><enddate>19950815</enddate><creator>Fromherz, Sylvia</creator><creator>Szent-Gyorgyi, Andrew G.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>5PM</scope></search><sort><creationdate>19950815</creationdate><title>Role of Essential Light Chain EF Hand Domains in Calcium Binding and Regulation of Scallop Myosin</title><author>Fromherz, Sylvia ; Szent-Gyorgyi, Andrew G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c586t-aa20d4758a3a6a665fa07158d42fdfa9c203d1ef3363afc2cf8c70a07e18ed53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine triphosphatases</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Calcium</topic><topic>Calcium - metabolism</topic><topic>Chimeras</topic><topic>Cloning, Molecular</topic><topic>Consensus Sequence</topic><topic>Divalent cations</topic><topic>Gels</topic><topic>Homeostasis</topic><topic>Hybridity</topic><topic>Marine</topic><topic>Molecular Sequence Data</topic><topic>Mollusca</topic><topic>Mollusks</topic><topic>Muscular system</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Myocardium - metabolism</topic><topic>Myosins - biosynthesis</topic><topic>Myosins - chemistry</topic><topic>Myosins - metabolism</topic><topic>Pectinidae</topic><topic>Physiological regulation</topic><topic>Polymerase Chain Reaction</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Scallops</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fromherz, Sylvia</creatorcontrib><creatorcontrib>Szent-Gyorgyi, Andrew G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fromherz, Sylvia</au><au>Szent-Gyorgyi, Andrew G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Essential Light Chain EF Hand Domains in Calcium Binding and Regulation of Scallop Myosin</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-08-15</date><risdate>1995</risdate><volume>92</volume><issue>17</issue><spage>7652</spage><epage>7656</epage><pages>7652-7656</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The specific Ca2+binding site that triggers contraction of molluscan muscle requires the presence of an essential light chain (ELC) from a Ca2+binding myosin. Of the four EF hand-like domains in molluscan ELCs, only domain III has an amino acid sequence predicted to be capable of binding Ca2+. In this report, we have used mutant ELCs to locate the Ca2+binding site in scallop myosin and to probe the role of the ELC in regulation. Point mutations in domain III of scallop ELC have no effect on Ca2+binding. Interestingly, scallop and rat cardiac ELC chimeras support Ca2+binding only if domain I is scallop. These results are nevertheless in agreement with structural studies on a proteolytic fragment of scallop myosin, the regulatory domain. Furthermore, Ca2+sensitivity of the scallop myosin ATPase requires scallop ELC domain I: ELCs containing cardiac domain I convert scallop myosin to an unregulated molecule whose activity is no longer repressed in the absence of Ca2+. Despite its unusual EF hand domain sequence, our data indicate that the unique and required contribution of molluscan ELCs to Ca2+binding and regulation of molluscan myosins resides exclusively in domain I.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7644472</pmid><doi>10.1073/pnas.92.17.7652</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine triphosphatases Amino Acid Sequence Amino acids Animals Binding Sites Biochemistry Calcium Calcium - metabolism Chimeras Cloning, Molecular Consensus Sequence Divalent cations Gels Homeostasis Hybridity Marine Molecular Sequence Data Mollusca Mollusks Muscular system Mutagenesis, Site-Directed Mutation Myocardium - metabolism Myosins - biosynthesis Myosins - chemistry Myosins - metabolism Pectinidae Physiological regulation Polymerase Chain Reaction Protein Binding Proteins Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism Scallops Sequence Homology, Amino Acid |
| title | Role of Essential Light Chain EF Hand Domains in Calcium Binding and Regulation of Scallop Myosin |
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