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The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne, D. J. (1989) J. Biol. Chem. 264, 13971-139...
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Published in: | The Journal of biological chemistry 1991-12, Vol.266 (35), p.23945-23952 |
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description | It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent
protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne,
D. J. (1989) J. Biol. Chem. 264, 13971-13974). In this study we have isolated and characterized cDNA and genomic clones encoding
telokin. Analysis of a genomic DNA clone suggests that the mRNA encoding telokin arises from a promoter which appears to be
located within an intron of the smooth muscle myosin light chain kinase (MLCK) gene. This intron interrupts exons encoding
the calmodulin binding domain of the kinase. The amino acid sequence deduced from the cDNA predicts that telokin is identical
to the carboxyl-terminal 155 residues of the smooth muscle MLCK. Unlike the smooth muscle MLCK which is expressed in both
smooth and non-muscle tissues, telokin is expressed in some smooth muscle tissues but has not been detected in aortic smooth
muscle or in any non-muscle tissues. |
doi_str_mv | 10.1016/s0021-9258(18)54376-3 |
format | article |
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protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne,
D. J. (1989) J. Biol. Chem. 264, 13971-13974). In this study we have isolated and characterized cDNA and genomic clones encoding
telokin. Analysis of a genomic DNA clone suggests that the mRNA encoding telokin arises from a promoter which appears to be
located within an intron of the smooth muscle myosin light chain kinase (MLCK) gene. This intron interrupts exons encoding
the calmodulin binding domain of the kinase. The amino acid sequence deduced from the cDNA predicts that telokin is identical
to the carboxyl-terminal 155 residues of the smooth muscle MLCK. Unlike the smooth muscle MLCK which is expressed in both
smooth and non-muscle tissues, telokin is expressed in some smooth muscle tissues but has not been detected in aortic smooth
muscle or in any non-muscle tissues.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)54376-3</identifier><identifier>PMID: 1748667</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Antibodies ; Base Sequence ; Biological and medical sciences ; C-terminus ; cDNA ; DNA - genetics ; DNA - isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Female ; Fundamental and applied biological sciences. Psychology ; genes ; Genomic Library ; Molecular Sequence Data ; Molecular Weight ; Muscle Proteins - genetics ; Muscle Proteins - isolation & purification ; Muscle, Smooth - enzymology ; myosin light chain kinase ; Myosin-Light-Chain Kinase - genetics ; nucleotide sequence ; Peptide Fragments ; Peptides ; predictions ; Rabbits ; Restriction Mapping ; smooth muscle ; telokin ; Transferases ; Uterus - enzymology</subject><ispartof>The Journal of biological chemistry, 1991-12, Vol.266 (35), p.23945-23952</ispartof><rights>1992 INIST-CNRS</rights><rights>1991 by The American Society for Biochemistry and Molecular Biology, Inc. 1991</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c561t-2bc84d1c975c3c17f6fdf1611d534884a1bc5265314f281e31d3a5e6d4c39f773</citedby><cites>FETCH-LOGICAL-c561t-2bc84d1c975c3c17f6fdf1611d534884a1bc5265314f281e31d3a5e6d4c39f773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5146843$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1748667$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>GALLAGHER, P. J</creatorcontrib><creatorcontrib>HERRING, B. P</creatorcontrib><title>The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent
protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne,
D. J. (1989) J. Biol. Chem. 264, 13971-13974). In this study we have isolated and characterized cDNA and genomic clones encoding
telokin. Analysis of a genomic DNA clone suggests that the mRNA encoding telokin arises from a promoter which appears to be
located within an intron of the smooth muscle myosin light chain kinase (MLCK) gene. This intron interrupts exons encoding
the calmodulin binding domain of the kinase. The amino acid sequence deduced from the cDNA predicts that telokin is identical
to the carboxyl-terminal 155 residues of the smooth muscle MLCK. Unlike the smooth muscle MLCK which is expressed in both
smooth and non-muscle tissues, telokin is expressed in some smooth muscle tissues but has not been detected in aortic smooth
muscle or in any non-muscle tissues.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>C-terminus</subject><subject>cDNA</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genomic Library</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle Proteins - isolation & purification</subject><subject>Muscle, Smooth - enzymology</subject><subject>myosin light chain kinase</subject><subject>Myosin-Light-Chain Kinase - genetics</subject><subject>nucleotide sequence</subject><subject>Peptide Fragments</subject><subject>Peptides</subject><subject>predictions</subject><subject>Rabbits</subject><subject>Restriction Mapping</subject><subject>smooth muscle</subject><subject>telokin</subject><subject>Transferases</subject><subject>Uterus - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><recordid>eNqFkU2L1TAYhYMo43X0JwxkIeKA1b75aroZkGH8gAEXjuAupGk6jbZNzdvq3H9vrvdyR1dmkQTOeU9OeAg5g_I1lKDeYFkyKGom9UvQ51LwShX8AdlAqXnBJXx9SDZHy2PyBPFbmZeo4YScQCW0UtWGLDe9p86mJt5tB7r4NIZpRRo7umQBxxiXno4rusHTcRsxTHQIt_1CXW_z_XuYLHoakPq7OXlE31KL1E40TK2ffd6mhc4pLj5Mr3L-EPPIU_KoswP6Z4fzlHx5d3Vz-aG4_vT-4-Xb68JJBUvBGqdFC66upOMOqk51bQcKoJVcaC0sNE4yJTmIjmnwHFpupVetcLzuqoqfkot97rw2o29d7pLsYOYURpu2Jtpg_lWm0Jvb-NMwzVWleA54cQhI8cfqcTFjQOeHwU4-rmgqJpUu6_K_RlCMMS5kNsq90aWImHx3bAOl2XE1n3fQzA6aAW3-cDW7Jmd_f-V-ag8y688PukVnhy7ZyQU82iQIpQW_t_UZ4q-QvGlCdL0fDVP5GWkYr3PL39qIuWU</recordid><startdate>19911215</startdate><enddate>19911215</enddate><creator>GALLAGHER, P. J</creator><creator>HERRING, B. P</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><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>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19911215</creationdate><title>The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin</title><author>GALLAGHER, P. J ; HERRING, B. P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c561t-2bc84d1c975c3c17f6fdf1611d534884a1bc5265314f281e31d3a5e6d4c39f773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>C-terminus</topic><topic>cDNA</topic><topic>DNA - genetics</topic><topic>DNA - isolation & purification</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genomic Library</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle Proteins - isolation & purification</topic><topic>Muscle, Smooth - enzymology</topic><topic>myosin light chain kinase</topic><topic>Myosin-Light-Chain Kinase - genetics</topic><topic>nucleotide sequence</topic><topic>Peptide Fragments</topic><topic>Peptides</topic><topic>predictions</topic><topic>Rabbits</topic><topic>Restriction Mapping</topic><topic>smooth muscle</topic><topic>telokin</topic><topic>Transferases</topic><topic>Uterus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GALLAGHER, P. J</creatorcontrib><creatorcontrib>HERRING, B. P</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>GALLAGHER, P. J</au><au>HERRING, B. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-12-15</date><risdate>1991</risdate><volume>266</volume><issue>35</issue><spage>23945</spage><epage>23952</epage><pages>23945-23952</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent
protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne,
D. J. (1989) J. Biol. Chem. 264, 13971-13974). In this study we have isolated and characterized cDNA and genomic clones encoding
telokin. Analysis of a genomic DNA clone suggests that the mRNA encoding telokin arises from a promoter which appears to be
located within an intron of the smooth muscle myosin light chain kinase (MLCK) gene. This intron interrupts exons encoding
the calmodulin binding domain of the kinase. The amino acid sequence deduced from the cDNA predicts that telokin is identical
to the carboxyl-terminal 155 residues of the smooth muscle MLCK. Unlike the smooth muscle MLCK which is expressed in both
smooth and non-muscle tissues, telokin is expressed in some smooth muscle tissues but has not been detected in aortic smooth
muscle or in any non-muscle tissues.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1748667</pmid><doi>10.1016/s0021-9258(18)54376-3</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Antibodies Base Sequence Biological and medical sciences C-terminus cDNA DNA - genetics DNA - isolation & purification Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology genes Genomic Library Molecular Sequence Data Molecular Weight Muscle Proteins - genetics Muscle Proteins - isolation & purification Muscle, Smooth - enzymology myosin light chain kinase Myosin-Light-Chain Kinase - genetics nucleotide sequence Peptide Fragments Peptides predictions Rabbits Restriction Mapping smooth muscle telokin Transferases Uterus - enzymology |
title | The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin |
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