Molecular Cloning of cDNAs Encoding Human Carnitine Acetyltransferase and Mapping of the Corresponding Gene to Chromosome 9q34.1
Using a combination of PCR screening of cDNA libraries and reverse transcription PCR, we have cloned three overlapping DNA fragments that encode human carnitine acetyltransferase (CAT), a key enzyme for metabolic pathways involved with the control of the acyl-CoA/CoA ratio in mitochondria, peroxisom...
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| Veröffentlicht in: | Genomics 1994-09, Vol.23 (1), p.94-99 |
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| creator | Corti, Olga Finocchiaro, Gaetano Rossi, Elena Zuffardi, Orsetta Didonato, Stefano |
| description | Using a combination of PCR screening of cDNA libraries and reverse transcription PCR, we have cloned three overlapping DNA fragments that encode human carnitine acetyltransferase (CAT), a key enzyme for metabolic pathways involved with the control of the acyl-CoA/CoA ratio in mitochondria, peroxisomes, and endoplasmic reticulum. The resulting cDNA (2436 bp) hybridizes to a mRNA species of ∼2.9 kb that is particularly abundant in skeletal muscle and encodes a 68-kDa protein containing a peroxisomal targeting signal. The sequence matches those of several tryptic peptides obtained from purified human liver CAT and shows striking similarities with other members of the carnitine/choline acetyltransferase family very distant throughout evolution. CAT cDNA has also been used for fluorescence in situ hybridization on metaphase spreads of human chromosomes, and the corresponding gene, CAT1 , has been mapped to chromosome 9q34.1. |
| doi_str_mv | 10.1006/geno.1994.1463 |
| format | Article |
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The resulting cDNA (2436 bp) hybridizes to a mRNA species of ∼2.9 kb that is particularly abundant in skeletal muscle and encodes a 68-kDa protein containing a peroxisomal targeting signal. The sequence matches those of several tryptic peptides obtained from purified human liver CAT and shows striking similarities with other members of the carnitine/choline acetyltransferase family very distant throughout evolution. CAT cDNA has also been used for fluorescence in situ hybridization on metaphase spreads of human chromosomes, and the corresponding gene, CAT1 , has been mapped to chromosome 9q34.1.</description><identifier>ISSN: 0888-7543</identifier><identifier>EISSN: 1089-8646</identifier><identifier>DOI: 10.1006/geno.1994.1463</identifier><identifier>PMID: 7829107</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>AMINO ACID SEQUENCE ; Base Sequence ; Biological and medical sciences ; BIOLOGICAL EVOLUTION ; BIOLOGY AND MEDICINE, BASIC STUDIES ; Blotting, Northern ; CARNITINE ; Carnitine O-Acetyltransferase - genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 9 ; Cloning, Molecular ; DNA ; DNA HYBRIDIZATION ; DNA SEQUENCING ; DNA, Complementary - genetics ; DNA-CLONING ; ELECTROPHORESIS ; ENZYMES ; ETIOLOGY ; FLUORESCENCE ; Fundamental and applied biological sciences. Psychology ; GENES ; Genes. Genome ; GENETIC MAPPING ; HUMAN CHROMOSOME 9 ; Humans ; In Situ Hybridization, Fluorescence ; MESSENGER-RNA ; METABOLIC DISEASES ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; NUCLEOTIDES ; PEPTIDES ; POLYMERASE CHAIN REACTION ; Sequence Alignment ; Sequence Homology, Amino Acid ; Species Specificity</subject><ispartof>Genomics, 1994-09, Vol.23 (1), p.94-99</ispartof><rights>1994 Academic Press</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-a80a764e0beb7497695c24e2a01b658ba3ff0d82ebd79cd332cccbf040547acd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/geno.1994.1463$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4249802$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7829107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/186058$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Corti, Olga</creatorcontrib><creatorcontrib>Finocchiaro, Gaetano</creatorcontrib><creatorcontrib>Rossi, Elena</creatorcontrib><creatorcontrib>Zuffardi, Orsetta</creatorcontrib><creatorcontrib>Didonato, Stefano</creatorcontrib><title>Molecular Cloning of cDNAs Encoding Human Carnitine Acetyltransferase and Mapping of the Corresponding Gene to Chromosome 9q34.1</title><title>Genomics</title><addtitle>Genomics</addtitle><description>Using a combination of PCR screening of cDNA libraries and reverse transcription PCR, we have cloned three overlapping DNA fragments that encode human carnitine acetyltransferase (CAT), a key enzyme for metabolic pathways involved with the control of the acyl-CoA/CoA ratio in mitochondria, peroxisomes, and endoplasmic reticulum. The resulting cDNA (2436 bp) hybridizes to a mRNA species of ∼2.9 kb that is particularly abundant in skeletal muscle and encodes a 68-kDa protein containing a peroxisomal targeting signal. The sequence matches those of several tryptic peptides obtained from purified human liver CAT and shows striking similarities with other members of the carnitine/choline acetyltransferase family very distant throughout evolution. CAT cDNA has also been used for fluorescence in situ hybridization on metaphase spreads of human chromosomes, and the corresponding gene, CAT1 , has been mapped to chromosome 9q34.1.</description><subject>AMINO ACID SEQUENCE</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>BIOLOGICAL EVOLUTION</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>Blotting, Northern</subject><subject>CARNITINE</subject><subject>Carnitine O-Acetyltransferase - genetics</subject><subject>Chromosome Mapping</subject><subject>Chromosomes, Human, Pair 9</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>DNA HYBRIDIZATION</subject><subject>DNA SEQUENCING</subject><subject>DNA, Complementary - genetics</subject><subject>DNA-CLONING</subject><subject>ELECTROPHORESIS</subject><subject>ENZYMES</subject><subject>ETIOLOGY</subject><subject>FLUORESCENCE</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENES</subject><subject>Genes. Genome</subject><subject>GENETIC MAPPING</subject><subject>HUMAN CHROMOSOME 9</subject><subject>Humans</subject><subject>In Situ Hybridization, Fluorescence</subject><subject>MESSENGER-RNA</subject><subject>METABOLIC DISEASES</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>NUCLEOTIDES</subject><subject>PEPTIDES</subject><subject>POLYMERASE CHAIN REACTION</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Species Specificity</subject><issn>0888-7543</issn><issn>1089-8646</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EKkvhyg3JSKi3LHbiOPZxFfqB1MIFzpbjTLpGiZ3aTqXe-NNx2Kg3xMnSzO89z8xD6D0le0oI_3wPzu-plGxPGa9eoB0lQhaCM_4S7YgQomhqVr1Gb2L8RQiRlSjP0FkjSklJs0O_7_wIZhl1wO3onXX32A_YfPl2iPjSGd-vlZtl0g63OjibrAN8MJCexhS0iwMEHQFr1-M7Pc-bPh0Btz4EiLN3fy2uIeuSx-0x-MlHPwGWD1Ue-i16NegxwrvtPUc_ry5_tDfF7ffrr-3htjCsrFOhBdENZ0A66BomGy5rUzIoNaEdr0Wnq2EgvSih6xtp-qoqjTHdQBipWaNz4Rx9PPn6mKyKxiYwR-OdA5MUFZzUIjMXJ2YO_mGBmNRko4Fx1A78EtX6qxCM_RekXNRciiaD-xNogo8xwKDmYCcdnhQlas1PrfmpNT-15pcFHzbnpZugf8a3wHL_09bX0ehxyBkYG58xVjIpSJkxccIgn_TRQlg3Bmegt2FduPf2XxP8AU8lttc</recordid><startdate>19940901</startdate><enddate>19940901</enddate><creator>Corti, Olga</creator><creator>Finocchiaro, Gaetano</creator><creator>Rossi, Elena</creator><creator>Zuffardi, Orsetta</creator><creator>Didonato, Stefano</creator><general>Elsevier Inc</general><general>Elsevier</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19940901</creationdate><title>Molecular Cloning of cDNAs Encoding Human Carnitine Acetyltransferase and Mapping of the Corresponding Gene to Chromosome 9q34.1</title><author>Corti, Olga ; Finocchiaro, Gaetano ; Rossi, Elena ; Zuffardi, Orsetta ; Didonato, Stefano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-a80a764e0beb7497695c24e2a01b658ba3ff0d82ebd79cd332cccbf040547acd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>AMINO ACID SEQUENCE</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>BIOLOGICAL EVOLUTION</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>Blotting, Northern</topic><topic>CARNITINE</topic><topic>Carnitine O-Acetyltransferase - genetics</topic><topic>Chromosome Mapping</topic><topic>Chromosomes, Human, Pair 9</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>DNA HYBRIDIZATION</topic><topic>DNA SEQUENCING</topic><topic>DNA, Complementary - genetics</topic><topic>DNA-CLONING</topic><topic>ELECTROPHORESIS</topic><topic>ENZYMES</topic><topic>ETIOLOGY</topic><topic>FLUORESCENCE</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENES</topic><topic>Genes. Genome</topic><topic>GENETIC MAPPING</topic><topic>HUMAN CHROMOSOME 9</topic><topic>Humans</topic><topic>In Situ Hybridization, Fluorescence</topic><topic>MESSENGER-RNA</topic><topic>METABOLIC DISEASES</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDES</topic><topic>PEPTIDES</topic><topic>POLYMERASE CHAIN REACTION</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Corti, Olga</creatorcontrib><creatorcontrib>Finocchiaro, Gaetano</creatorcontrib><creatorcontrib>Rossi, Elena</creatorcontrib><creatorcontrib>Zuffardi, Orsetta</creatorcontrib><creatorcontrib>Didonato, Stefano</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Genomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Corti, Olga</au><au>Finocchiaro, Gaetano</au><au>Rossi, Elena</au><au>Zuffardi, Orsetta</au><au>Didonato, Stefano</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning of cDNAs Encoding Human Carnitine Acetyltransferase and Mapping of the Corresponding Gene to Chromosome 9q34.1</atitle><jtitle>Genomics</jtitle><addtitle>Genomics</addtitle><date>1994-09-01</date><risdate>1994</risdate><volume>23</volume><issue>1</issue><spage>94</spage><epage>99</epage><pages>94-99</pages><issn>0888-7543</issn><eissn>1089-8646</eissn><abstract>Using a combination of PCR screening of cDNA libraries and reverse transcription PCR, we have cloned three overlapping DNA fragments that encode human carnitine acetyltransferase (CAT), a key enzyme for metabolic pathways involved with the control of the acyl-CoA/CoA ratio in mitochondria, peroxisomes, and endoplasmic reticulum. The resulting cDNA (2436 bp) hybridizes to a mRNA species of ∼2.9 kb that is particularly abundant in skeletal muscle and encodes a 68-kDa protein containing a peroxisomal targeting signal. The sequence matches those of several tryptic peptides obtained from purified human liver CAT and shows striking similarities with other members of the carnitine/choline acetyltransferase family very distant throughout evolution. CAT cDNA has also been used for fluorescence in situ hybridization on metaphase spreads of human chromosomes, and the corresponding gene, CAT1 , has been mapped to chromosome 9q34.1.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>7829107</pmid><doi>10.1006/geno.1994.1463</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Genomics, 1994-09, Vol.23 (1), p.94-99 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | AMINO ACID SEQUENCE Base Sequence Biological and medical sciences BIOLOGICAL EVOLUTION BIOLOGY AND MEDICINE, BASIC STUDIES Blotting, Northern CARNITINE Carnitine O-Acetyltransferase - genetics Chromosome Mapping Chromosomes, Human, Pair 9 Cloning, Molecular DNA DNA HYBRIDIZATION DNA SEQUENCING DNA, Complementary - genetics DNA-CLONING ELECTROPHORESIS ENZYMES ETIOLOGY FLUORESCENCE Fundamental and applied biological sciences. Psychology GENES Genes. Genome GENETIC MAPPING HUMAN CHROMOSOME 9 Humans In Situ Hybridization, Fluorescence MESSENGER-RNA METABOLIC DISEASES Molecular and cellular biology Molecular genetics Molecular Sequence Data NUCLEOTIDES PEPTIDES POLYMERASE CHAIN REACTION Sequence Alignment Sequence Homology, Amino Acid Species Specificity |
| title | Molecular Cloning of cDNAs Encoding Human Carnitine Acetyltransferase and Mapping of the Corresponding Gene to Chromosome 9q34.1 |
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