Two Distinct Genes for ADP/ATP Translocase are Expressed at the mRNA Level in Adult Human Liver
Several clones hybridizing with a bovine ADP/ATP translocase cDNA were isolated from an adult human liver cDNA library in the vector pEX1. DNA sequence analysis revealed that these clones encode two distinct forms of translocase. In particular, two clones specifying the COOH-end-proximal five-sixths...
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| Veröffentlicht in: | Proc. Natl. Acad. Sci. U.S.A.; (United States) 1988, Vol.85 (2), p.377-381 |
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| description | Several clones hybridizing with a bovine ADP/ATP translocase cDNA were isolated from an adult human liver cDNA library in the vector pEX1. DNA sequence analysis revealed that these clones encode two distinct forms of translocase. In particular, two clones specifying the COOH-end-proximal five-sixths of the protein exhibit a 9% amino acid sequence divergence and totally dissimilar 3′ untranslated regions. One of these cDNAs is nearly identical in sequence to an ADP/ATP translocase clone (hp2F1) recently isolated from a human fibroblast cDNA library [Battini, R., Ferrari, S., Kaczmarek, L., Calabretta, B., Chen, S. & Baserga, R. (1987) J. Biol. Chem. 262, 4355-4359], with three amino acid changes and a few differences in the 3′ untranslated region. Another clone isolated from the pEX1 library contains a reading frame encoding the remaining, NH2-end-proximal, 37 amino acids of the translocase. This sequence differs significantly (14% amino acid sequence divergence) from the corresponding segment of hp2F1, and the 5′ untranslated regions of the two clones are totally dissimilar. RNA transfer hybridization experiments utilizing the clones isolated from the pEX1 library revealed the presence in HeLa cells of three distinct mRNA species. The pattern of hybridization and the sizes of these mRNAs suggest a greater complexity of organization and expression of the ADP/ATP translocase genes in human cells than indicated by the analysis of the cDNA clones. |
| doi_str_mv | 10.1073/pnas.85.2.377 |
| format | Article |
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DNA sequence analysis revealed that these clones encode two distinct forms of translocase. In particular, two clones specifying the COOH-end-proximal five-sixths of the protein exhibit a 9% amino acid sequence divergence and totally dissimilar 3′ untranslated regions. One of these cDNAs is nearly identical in sequence to an ADP/ATP translocase clone (hp2F1) recently isolated from a human fibroblast cDNA library [Battini, R., Ferrari, S., Kaczmarek, L., Calabretta, B., Chen, S. & Baserga, R. (1987) J. Biol. Chem. 262, 4355-4359], with three amino acid changes and a few differences in the 3′ untranslated region. Another clone isolated from the pEX1 library contains a reading frame encoding the remaining, NH2-end-proximal, 37 amino acids of the translocase. This sequence differs significantly (14% amino acid sequence divergence) from the corresponding segment of hp2F1, and the 5′ untranslated regions of the two clones are totally dissimilar. RNA transfer hybridization experiments utilizing the clones isolated from the pEX1 library revealed the presence in HeLa cells of three distinct mRNA species. The pattern of hybridization and the sizes of these mRNAs suggest a greater complexity of organization and expression of the ADP/ATP translocase genes in human cells than indicated by the analysis of the cDNA clones.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.85.2.377</identifier><identifier>PMID: 2829183</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>550201 - Biochemistry- Tracer Techniques ; ACID ANHYDRASES ; Adult ; ADULTS ; AGE GROUPS ; AMINO ACID SEQUENCE ; Amino acids ; ANIMAL CELLS ; Animals ; ATP ; ATP-ASE ; Base Sequence ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BETA-MINUS DECAY RADIOISOTOPES ; Biological and medical sciences ; BODY ; Cattle ; CELL CONSTITUENTS ; CELL MEMBRANES ; Cloning, Molecular ; Complementary DNA ; CONNECTIVE TISSUE CELLS ; DAYS LIVING RADIOISOTOPES ; DIGESTIVE SYSTEM ; DNA ; DNA Restriction Enzymes ; DNA SEQUENCING ; ENZYMES ; EVEN-ODD NUCLEI ; FIBROBLASTS ; Fundamental and applied biological sciences. Psychology ; Gene expression ; GENES ; Genetic hybridization ; GLANDS ; HELA CELLS ; Humans ; HYBRIDIZATION ; HYDROLASES ; ISOTOPES ; LIGHT NUCLEI ; LIVER ; Liver - metabolism ; MEMBRANES ; MESSENGER-RNA ; MITOCHONDRIA ; Mitochondrial ADP, ATP Translocases - genetics ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; MOLECULAR STRUCTURE ; NUCLEI ; Nucleic Acid Hybridization ; NUCLEIC ACIDS ; NUCLEOTIDES ; Nucleotidyltransferases - genetics ; ODD-ODD NUCLEI ; ORGANIC COMPOUNDS ; ORGANOIDS ; ORGANS ; PHOSPHOHYDROLASES ; PHOSPHORUS 32 ; PHOSPHORUS ISOTOPES ; RADIOISOTOPES ; Reading frames ; RECOMBINANT DNA ; RNA ; RNA, Messenger - genetics ; Sequence Homology, Nucleic Acid ; SOMATIC CELLS ; Species Specificity ; STRUCTURAL CHEMICAL ANALYSIS ; SULFUR 35 ; SULFUR ISOTOPES ; Three prime untranslated regions ; Transcription, Genetic ; Ungulates</subject><ispartof>Proc. Natl. Acad. Sci. U.S.A.; (United States), 1988, Vol.85 (2), p.377-381</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4637-bd8022d033ec704133a0415d92cc46ef5adb7cdc76cf068c2e65b6136ae800d13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/85/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/31162$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/31162$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,885,4022,27922,27923,27924,58016,58249</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7562468$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2829183$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6143394$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Houldsworth, Jane</creatorcontrib><creatorcontrib>Attardi, Giuseppe</creatorcontrib><creatorcontrib>California Institute of Technology, Pasadena (USA)</creatorcontrib><title>Two Distinct Genes for ADP/ATP Translocase are Expressed at the mRNA Level in Adult Human Liver</title><title>Proc. Natl. Acad. Sci. U.S.A.; (United States)</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Several clones hybridizing with a bovine ADP/ATP translocase cDNA were isolated from an adult human liver cDNA library in the vector pEX1. DNA sequence analysis revealed that these clones encode two distinct forms of translocase. In particular, two clones specifying the COOH-end-proximal five-sixths of the protein exhibit a 9% amino acid sequence divergence and totally dissimilar 3′ untranslated regions. One of these cDNAs is nearly identical in sequence to an ADP/ATP translocase clone (hp2F1) recently isolated from a human fibroblast cDNA library [Battini, R., Ferrari, S., Kaczmarek, L., Calabretta, B., Chen, S. & Baserga, R. (1987) J. Biol. Chem. 262, 4355-4359], with three amino acid changes and a few differences in the 3′ untranslated region. Another clone isolated from the pEX1 library contains a reading frame encoding the remaining, NH2-end-proximal, 37 amino acids of the translocase. This sequence differs significantly (14% amino acid sequence divergence) from the corresponding segment of hp2F1, and the 5′ untranslated regions of the two clones are totally dissimilar. RNA transfer hybridization experiments utilizing the clones isolated from the pEX1 library revealed the presence in HeLa cells of three distinct mRNA species. The pattern of hybridization and the sizes of these mRNAs suggest a greater complexity of organization and expression of the ADP/ATP translocase genes in human cells than indicated by the analysis of the cDNA clones.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>ACID ANHYDRASES</subject><subject>Adult</subject><subject>ADULTS</subject><subject>AGE GROUPS</subject><subject>AMINO ACID SEQUENCE</subject><subject>Amino acids</subject><subject>ANIMAL CELLS</subject><subject>Animals</subject><subject>ATP</subject><subject>ATP-ASE</subject><subject>Base Sequence</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BETA DECAY RADIOISOTOPES</subject><subject>BETA-MINUS DECAY RADIOISOTOPES</subject><subject>Biological and medical sciences</subject><subject>BODY</subject><subject>Cattle</subject><subject>CELL CONSTITUENTS</subject><subject>CELL MEMBRANES</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>CONNECTIVE TISSUE CELLS</subject><subject>DAYS LIVING RADIOISOTOPES</subject><subject>DIGESTIVE SYSTEM</subject><subject>DNA</subject><subject>DNA Restriction Enzymes</subject><subject>DNA SEQUENCING</subject><subject>ENZYMES</subject><subject>EVEN-ODD NUCLEI</subject><subject>FIBROBLASTS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>GENES</subject><subject>Genetic hybridization</subject><subject>GLANDS</subject><subject>HELA CELLS</subject><subject>Humans</subject><subject>HYBRIDIZATION</subject><subject>HYDROLASES</subject><subject>ISOTOPES</subject><subject>LIGHT NUCLEI</subject><subject>LIVER</subject><subject>Liver - metabolism</subject><subject>MEMBRANES</subject><subject>MESSENGER-RNA</subject><subject>MITOCHONDRIA</subject><subject>Mitochondrial ADP, ATP Translocases - genetics</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>MOLECULAR STRUCTURE</subject><subject>NUCLEI</subject><subject>Nucleic Acid Hybridization</subject><subject>NUCLEIC ACIDS</subject><subject>NUCLEOTIDES</subject><subject>Nucleotidyltransferases - genetics</subject><subject>ODD-ODD NUCLEI</subject><subject>ORGANIC COMPOUNDS</subject><subject>ORGANOIDS</subject><subject>ORGANS</subject><subject>PHOSPHOHYDROLASES</subject><subject>PHOSPHORUS 32</subject><subject>PHOSPHORUS ISOTOPES</subject><subject>RADIOISOTOPES</subject><subject>Reading frames</subject><subject>RECOMBINANT DNA</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>SOMATIC CELLS</subject><subject>Species Specificity</subject><subject>STRUCTURAL CHEMICAL ANALYSIS</subject><subject>SULFUR 35</subject><subject>SULFUR ISOTOPES</subject><subject>Three prime untranslated regions</subject><subject>Transcription, Genetic</subject><subject>Ungulates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90E1v1DAQBmALgcpSOHJBIFmI9patPxLbOUZtaSutoELL2fI6EzVVPhaPU9p_X682XXHi4jm8j2bkl5CPnC050_JsOzhcmmIpllLrV2TBWckzlZfsNVkwJnRmcpG_Je8Q7xljZWHYETkSRpTcyAWx678jvWgxtoOP9AoGQNqMgVYXt2fV-paugxuwG71DoC4AvXzcBkCEmrpI4x3Q_tePiq7gATraDrSqpy7S66l3A121DxDekzeN6xA-zPOY_P5-uT6_zlY_r27Oq1XmcyV1tqkNE6JmUoLXLOdSuvQWdSl8AtAUrt5oX3utfMOU8QJUsVFcKgeGsZrLY_J1v3dMX7Ho2wj-zo_DAD5axXMpyzyh0z3ahvHPBBht36KHrnMDjBNabVJ5TJsEsz30YUQM0NhtaHsXnixndte63bVuTWGFTa0n_2VePG16qA96rjnl3-bcoXddk0r1LR6YLpTI1e7s55nttr-k_1w5-U9sm6nrIjzG5D7t3T3GMRyg5FwJ-QwUAafo</recordid><startdate>1988</startdate><enddate>1988</enddate><creator>Houldsworth, Jane</creator><creator>Attardi, Giuseppe</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>1988</creationdate><title>Two Distinct Genes for ADP/ATP Translocase are Expressed at the mRNA Level in Adult Human Liver</title><author>Houldsworth, Jane ; Attardi, Giuseppe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4637-bd8022d033ec704133a0415d92cc46ef5adb7cdc76cf068c2e65b6136ae800d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>ACID ANHYDRASES</topic><topic>Adult</topic><topic>ADULTS</topic><topic>AGE GROUPS</topic><topic>AMINO ACID SEQUENCE</topic><topic>Amino acids</topic><topic>ANIMAL CELLS</topic><topic>Animals</topic><topic>ATP</topic><topic>ATP-ASE</topic><topic>Base Sequence</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BETA DECAY RADIOISOTOPES</topic><topic>BETA-MINUS DECAY RADIOISOTOPES</topic><topic>Biological and medical sciences</topic><topic>BODY</topic><topic>Cattle</topic><topic>CELL CONSTITUENTS</topic><topic>CELL MEMBRANES</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>CONNECTIVE TISSUE CELLS</topic><topic>DAYS LIVING RADIOISOTOPES</topic><topic>DIGESTIVE SYSTEM</topic><topic>DNA</topic><topic>DNA Restriction Enzymes</topic><topic>DNA SEQUENCING</topic><topic>ENZYMES</topic><topic>EVEN-ODD NUCLEI</topic><topic>FIBROBLASTS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>GENES</topic><topic>Genetic hybridization</topic><topic>GLANDS</topic><topic>HELA CELLS</topic><topic>Humans</topic><topic>HYBRIDIZATION</topic><topic>HYDROLASES</topic><topic>ISOTOPES</topic><topic>LIGHT NUCLEI</topic><topic>LIVER</topic><topic>Liver - metabolism</topic><topic>MEMBRANES</topic><topic>MESSENGER-RNA</topic><topic>MITOCHONDRIA</topic><topic>Mitochondrial ADP, ATP Translocases - genetics</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>MOLECULAR STRUCTURE</topic><topic>NUCLEI</topic><topic>Nucleic Acid Hybridization</topic><topic>NUCLEIC ACIDS</topic><topic>NUCLEOTIDES</topic><topic>Nucleotidyltransferases - genetics</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>ORGANOIDS</topic><topic>ORGANS</topic><topic>PHOSPHOHYDROLASES</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>RADIOISOTOPES</topic><topic>Reading frames</topic><topic>RECOMBINANT DNA</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>SOMATIC CELLS</topic><topic>Species Specificity</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><topic>SULFUR 35</topic><topic>SULFUR ISOTOPES</topic><topic>Three prime untranslated regions</topic><topic>Transcription, Genetic</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Houldsworth, Jane</creatorcontrib><creatorcontrib>Attardi, Giuseppe</creatorcontrib><creatorcontrib>California Institute of Technology, Pasadena (USA)</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>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Houldsworth, Jane</au><au>Attardi, Giuseppe</au><aucorp>California Institute of Technology, Pasadena (USA)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two Distinct Genes for ADP/ATP Translocase are Expressed at the mRNA Level in Adult Human Liver</atitle><jtitle>Proc. Natl. Acad. Sci. U.S.A.; (United States)</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1988</date><risdate>1988</risdate><volume>85</volume><issue>2</issue><spage>377</spage><epage>381</epage><pages>377-381</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Several clones hybridizing with a bovine ADP/ATP translocase cDNA were isolated from an adult human liver cDNA library in the vector pEX1. DNA sequence analysis revealed that these clones encode two distinct forms of translocase. In particular, two clones specifying the COOH-end-proximal five-sixths of the protein exhibit a 9% amino acid sequence divergence and totally dissimilar 3′ untranslated regions. One of these cDNAs is nearly identical in sequence to an ADP/ATP translocase clone (hp2F1) recently isolated from a human fibroblast cDNA library [Battini, R., Ferrari, S., Kaczmarek, L., Calabretta, B., Chen, S. & Baserga, R. (1987) J. Biol. Chem. 262, 4355-4359], with three amino acid changes and a few differences in the 3′ untranslated region. Another clone isolated from the pEX1 library contains a reading frame encoding the remaining, NH2-end-proximal, 37 amino acids of the translocase. This sequence differs significantly (14% amino acid sequence divergence) from the corresponding segment of hp2F1, and the 5′ untranslated regions of the two clones are totally dissimilar. RNA transfer hybridization experiments utilizing the clones isolated from the pEX1 library revealed the presence in HeLa cells of three distinct mRNA species. The pattern of hybridization and the sizes of these mRNAs suggest a greater complexity of organization and expression of the ADP/ATP translocase genes in human cells than indicated by the analysis of the cDNA clones.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2829183</pmid><doi>10.1073/pnas.85.2.377</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proc. Natl. Acad. Sci. U.S.A.; (United States), 1988, Vol.85 (2), p.377-381 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pascalfrancis_primary_7562468 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 550201 - Biochemistry- Tracer Techniques ACID ANHYDRASES Adult ADULTS AGE GROUPS AMINO ACID SEQUENCE Amino acids ANIMAL CELLS Animals ATP ATP-ASE Base Sequence BASIC BIOLOGICAL SCIENCES BETA DECAY RADIOISOTOPES BETA-MINUS DECAY RADIOISOTOPES Biological and medical sciences BODY Cattle CELL CONSTITUENTS CELL MEMBRANES Cloning, Molecular Complementary DNA CONNECTIVE TISSUE CELLS DAYS LIVING RADIOISOTOPES DIGESTIVE SYSTEM DNA DNA Restriction Enzymes DNA SEQUENCING ENZYMES EVEN-ODD NUCLEI FIBROBLASTS Fundamental and applied biological sciences. Psychology Gene expression GENES Genetic hybridization GLANDS HELA CELLS Humans HYBRIDIZATION HYDROLASES ISOTOPES LIGHT NUCLEI LIVER Liver - metabolism MEMBRANES MESSENGER-RNA MITOCHONDRIA Mitochondrial ADP, ATP Translocases - genetics Molecular and cellular biology Molecular genetics Molecular Sequence Data MOLECULAR STRUCTURE NUCLEI Nucleic Acid Hybridization NUCLEIC ACIDS NUCLEOTIDES Nucleotidyltransferases - genetics ODD-ODD NUCLEI ORGANIC COMPOUNDS ORGANOIDS ORGANS PHOSPHOHYDROLASES PHOSPHORUS 32 PHOSPHORUS ISOTOPES RADIOISOTOPES Reading frames RECOMBINANT DNA RNA RNA, Messenger - genetics Sequence Homology, Nucleic Acid SOMATIC CELLS Species Specificity STRUCTURAL CHEMICAL ANALYSIS SULFUR 35 SULFUR ISOTOPES Three prime untranslated regions Transcription, Genetic Ungulates |
| title | Two Distinct Genes for ADP/ATP Translocase are Expressed at the mRNA Level in Adult Human Liver |
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