Roles of Light Chains in the Activity and Conformation of Smooth Muscle Myosin
The 20-kDa regulatory (LC20) and 17-kDa essential (LC17) light chain subunits could be removed from porcine aorta smooth muscle myosin by the use of trifluoperazine and ammonium chloride. The isolated heavy chain rebound both light chains, resulting in the restoration of native properties. Experimen...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-04, Vol.271 (17), p.9992-9996 |
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| container_title | The Journal of biological chemistry |
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| creator | Katoh, T Morita, F |
| description | The 20-kDa regulatory (LC20) and 17-kDa essential (LC17) light chain subunits could be removed from porcine aorta smooth muscle
myosin by the use of trifluoperazine and ammonium chloride. The isolated heavy chain rebound both light chains, resulting
in the restoration of native properties. Experiments on reconstitution of the isolated heavy chain with LC17 and/or LC20 showed
that both light chains were required for folding into the 10 S conformation and thus for the phosphorylation-dependent filament
formation of smooth muscle myosin. However, LC17 was not essential for the phosphorylation-dependent regulation of actin-activated
ATPase activity and superprecipitation but was required for full regulation. LC17 and phosphorylated LC20 were found to act
as activators, and dephosphorylated LC20 was found to act as a repressor of the motor activities of smooth muscle myosin. |
| doi_str_mv | 10.1074/jbc.271.17.9992 |
| format | Article |
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myosin by the use of trifluoperazine and ammonium chloride. The isolated heavy chain rebound both light chains, resulting
in the restoration of native properties. Experiments on reconstitution of the isolated heavy chain with LC17 and/or LC20 showed
that both light chains were required for folding into the 10 S conformation and thus for the phosphorylation-dependent filament
formation of smooth muscle myosin. However, LC17 was not essential for the phosphorylation-dependent regulation of actin-activated
ATPase activity and superprecipitation but was required for full regulation. LC17 and phosphorylated LC20 were found to act
as activators, and dephosphorylated LC20 was found to act as a repressor of the motor activities of smooth muscle myosin.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.17.9992</identifier><identifier>PMID: 8626639</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Actins - metabolism ; Animals ; Aorta - enzymology ; Chemical Precipitation ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Microscopy, Electron ; Muscle, Smooth, Vascular - enzymology ; Myosin Light Chains - chemistry ; Myosins - chemistry ; Myosins - metabolism ; Protein Conformation ; Structure-Activity Relationship ; Swine</subject><ispartof>The Journal of biological chemistry, 1996-04, Vol.271 (17), p.9992-9996</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-76d66d84c19876aa5a85b6a74a143a11297cde8b9a805ec80ee810ce226b030d3</citedby><cites>FETCH-LOGICAL-c427t-76d66d84c19876aa5a85b6a74a143a11297cde8b9a805ec80ee810ce226b030d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8626639$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Katoh, T</creatorcontrib><creatorcontrib>Morita, F</creatorcontrib><title>Roles of Light Chains in the Activity and Conformation of Smooth Muscle Myosin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The 20-kDa regulatory (LC20) and 17-kDa essential (LC17) light chain subunits could be removed from porcine aorta smooth muscle
myosin by the use of trifluoperazine and ammonium chloride. The isolated heavy chain rebound both light chains, resulting
in the restoration of native properties. Experiments on reconstitution of the isolated heavy chain with LC17 and/or LC20 showed
that both light chains were required for folding into the 10 S conformation and thus for the phosphorylation-dependent filament
formation of smooth muscle myosin. However, LC17 was not essential for the phosphorylation-dependent regulation of actin-activated
ATPase activity and superprecipitation but was required for full regulation. LC17 and phosphorylated LC20 were found to act
as activators, and dephosphorylated LC20 was found to act as a repressor of the motor activities of smooth muscle myosin.</description><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Aorta - enzymology</subject><subject>Chemical Precipitation</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Enzyme Activation</subject><subject>Microscopy, Electron</subject><subject>Muscle, Smooth, Vascular - enzymology</subject><subject>Myosin Light Chains - chemistry</subject><subject>Myosins - chemistry</subject><subject>Myosins - metabolism</subject><subject>Protein Conformation</subject><subject>Structure-Activity Relationship</subject><subject>Swine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtLw0AUhQdRaq2uXQkDgrukcyfJPJal-IJWwQe4GyaTiZmSZGomVfrvTWkRvJu7ON85iw-hSyAxEJ5OV7mJKYcYeCylpEdoDEQkUZLBxzEaE0IhkjQTp-gshBUZLpUwQiPBKGOJHKOnF1_bgH2JF-6z6vG80q4N2LW4ryyemd59u36LdVvguW9L3zW6d77dFV4b7_sKLzfB1BYvtz649hydlLoO9uLwJ-j97vZt_hAtnu8f57NFZFLK-4izgrFCpAak4EzrTIssZ5qnGtJEA1DJTWFFLrUgmTWCWCuAGEspy0lCimSCbva7685_bWzoVeOCsXWtW-s3QXFBKOcAAzjdg6bzIXS2VOvONbrbKiBqZ1ANBtVgUAFXO4ND4-owvckbW_zxB2VDfr3Pq0HYj-usyp03lW3-rfwC2Lh3Qg</recordid><startdate>19960426</startdate><enddate>19960426</enddate><creator>Katoh, T</creator><creator>Morita, F</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19960426</creationdate><title>Roles of Light Chains in the Activity and Conformation of Smooth Muscle Myosin</title><author>Katoh, T ; Morita, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-76d66d84c19876aa5a85b6a74a143a11297cde8b9a805ec80ee810ce226b030d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Aorta - enzymology</topic><topic>Chemical Precipitation</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Enzyme Activation</topic><topic>Microscopy, Electron</topic><topic>Muscle, Smooth, Vascular - enzymology</topic><topic>Myosin Light Chains - chemistry</topic><topic>Myosins - chemistry</topic><topic>Myosins - metabolism</topic><topic>Protein Conformation</topic><topic>Structure-Activity Relationship</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Katoh, T</creatorcontrib><creatorcontrib>Morita, F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Katoh, T</au><au>Morita, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Roles of Light Chains in the Activity and Conformation of Smooth Muscle Myosin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-04-26</date><risdate>1996</risdate><volume>271</volume><issue>17</issue><spage>9992</spage><epage>9996</epage><pages>9992-9996</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The 20-kDa regulatory (LC20) and 17-kDa essential (LC17) light chain subunits could be removed from porcine aorta smooth muscle
myosin by the use of trifluoperazine and ammonium chloride. The isolated heavy chain rebound both light chains, resulting
in the restoration of native properties. Experiments on reconstitution of the isolated heavy chain with LC17 and/or LC20 showed
that both light chains were required for folding into the 10 S conformation and thus for the phosphorylation-dependent filament
formation of smooth muscle myosin. However, LC17 was not essential for the phosphorylation-dependent regulation of actin-activated
ATPase activity and superprecipitation but was required for full regulation. LC17 and phosphorylated LC20 were found to act
as activators, and dephosphorylated LC20 was found to act as a repressor of the motor activities of smooth muscle myosin.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8626639</pmid><doi>10.1074/jbc.271.17.9992</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1996-04, Vol.271 (17), p.9992-9996 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78027711 |
| source | MEDLINE; EZB Free E-Journals; Alma/SFX Local Collection |
| subjects | Actins - metabolism Animals Aorta - enzymology Chemical Precipitation Chromatography, High Pressure Liquid Enzyme Activation Microscopy, Electron Muscle, Smooth, Vascular - enzymology Myosin Light Chains - chemistry Myosins - chemistry Myosins - metabolism Protein Conformation Structure-Activity Relationship Swine |
| title | Roles of Light Chains in the Activity and Conformation of Smooth Muscle Myosin |
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