Molecular Cloning and Nucleotide Sequence of Rat Kidney γ -glutamyl Transpeptidase cDNA
We have screened a cDNA library (20,000 clones) made from rat kidney poly(A)+ RNA, using an oligonucleotide probe that was a mixture of 14-base DNA oligomers containing all 32 possible sequences coding for residues 32-36 of the γ -glutamyl transpeptidase (EC 2.3.2.2.) heavy chain. We isolated and se...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1986-02, Vol.83 (4), p.937-941 |
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creator | Laperche, Yannick Bulle, Frédérique Aissani, Tsouria Chobert, Marie-Noëlle Aggerbeck, Martine Hanoune, Jacques Guellaen, Georges |
description | We have screened a cDNA library (20,000 clones) made from rat kidney poly(A)+ RNA, using an oligonucleotide probe that was a mixture of 14-base DNA oligomers containing all 32 possible sequences coding for residues 32-36 of the γ -glutamyl transpeptidase (EC 2.3.2.2.) heavy chain. We isolated and sequenced two cDNAs corresponding to the mRNA coding for the entire length of the enzyme precursor. The nucleotide sequence that we obtained (2072 bases) reveals an open reading frame of 1707 nucleotides coding for the common precursor of both enzyme subunits. The amino acid sequence begins with the 21 residues located at the NH2-terminal hydrophobic region of the heavy subunit. We show that this sequence, which is not processed, is the only possible signal peptide in the sequence. Five potential N-glycosylation sites are present in the γ -glutamyl transpeptidase sequence. Using one of the two cDNA clones as probe, a 2.2-kilobase sequence was detected by blot analysis in rat kidney and human fetal liver RNA. |
doi_str_mv | 10.1073/pnas.83.4.937 |
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We isolated and sequenced two cDNAs corresponding to the mRNA coding for the entire length of the enzyme precursor. The nucleotide sequence that we obtained (2072 bases) reveals an open reading frame of 1707 nucleotides coding for the common precursor of both enzyme subunits. The amino acid sequence begins with the 21 residues located at the NH2-terminal hydrophobic region of the heavy subunit. We show that this sequence, which is not processed, is the only possible signal peptide in the sequence. Five potential N-glycosylation sites are present in the γ -glutamyl transpeptidase sequence. Using one of the two cDNA clones as probe, a 2.2-kilobase sequence was detected by blot analysis in rat kidney and human fetal liver RNA.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.83.4.937</identifier><identifier>PMID: 2869484</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Cloning, Molecular ; Complementary DNA ; DNA ; DNA - analysis ; DNA, Recombinant - analysis ; Enzymes ; Fundamental and applied biological sciences. Psychology ; gamma-Glutamyltransferase - genetics ; Genetic engineering ; Genetic technics ; Kidney - analysis ; Kidneys ; Liver ; Messenger RNA ; Methods. Procedures. Technologies ; Molecular cloning ; Nucleotide sequences ; Nucleotides ; Poly A - genetics ; Protein Precursors - genetics ; Protein Sorting Signals - genetics ; Rats ; RNA ; RNA, Messenger - genetics</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1986-02, Vol.83 (4), p.937-941</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4617-1d45308b4aa1e8b776d122a45246d90d5c4eeded9dd4a5106d46782ec3aea14f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/83/4.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/27069$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/27069$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8608895$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2869484$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Laperche, Yannick</creatorcontrib><creatorcontrib>Bulle, Frédérique</creatorcontrib><creatorcontrib>Aissani, Tsouria</creatorcontrib><creatorcontrib>Chobert, Marie-Noëlle</creatorcontrib><creatorcontrib>Aggerbeck, Martine</creatorcontrib><creatorcontrib>Hanoune, Jacques</creatorcontrib><creatorcontrib>Guellaen, Georges</creatorcontrib><title>Molecular Cloning and Nucleotide Sequence of Rat Kidney γ -glutamyl Transpeptidase cDNA</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have screened a cDNA library (20,000 clones) made from rat kidney poly(A)+ RNA, using an oligonucleotide probe that was a mixture of 14-base DNA oligomers containing all 32 possible sequences coding for residues 32-36 of the γ -glutamyl transpeptidase (EC 2.3.2.2.) heavy chain. We isolated and sequenced two cDNAs corresponding to the mRNA coding for the entire length of the enzyme precursor. The nucleotide sequence that we obtained (2072 bases) reveals an open reading frame of 1707 nucleotides coding for the common precursor of both enzyme subunits. The amino acid sequence begins with the 21 residues located at the NH2-terminal hydrophobic region of the heavy subunit. We show that this sequence, which is not processed, is the only possible signal peptide in the sequence. Five potential N-glycosylation sites are present in the γ -glutamyl transpeptidase sequence. Using one of the two cDNA clones as probe, a 2.2-kilobase sequence was detected by blot analysis in rat kidney and human fetal liver RNA.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>DNA</subject><subject>DNA - analysis</subject><subject>DNA, Recombinant - analysis</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gamma-Glutamyltransferase - genetics</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Kidney - analysis</subject><subject>Kidneys</subject><subject>Liver</subject><subject>Messenger RNA</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular cloning</subject><subject>Nucleotide sequences</subject><subject>Nucleotides</subject><subject>Poly A - genetics</subject><subject>Protein Precursors - genetics</subject><subject>Protein Sorting Signals - genetics</subject><subject>Rats</subject><subject>RNA</subject><subject>RNA, Messenger - genetics</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kTuP1DAUhS0EWoaFkgaB5ALoMvgVP4otVsNTLIsEi0RneeybISuPHeIEMb-L_8FvIqOJZqGhcnG-c-_xPQg9pGRJieIvuuTKUvOlWBqubqEFJYZWUhhyGy0IYarSgom76F4p14QQU2tygk6YlkZosUBfP-QIfoyux6uYU5s22KWAL0cfIQ9tAPwZvo-QPODc4E9uwO_bkGCHf__C1SaOg9vuIr7qXSoddJPBFcD-5eX5fXSncbHAg_k9RV9ev7pava0uPr55tzq_qLyQVFU0iJoTvRbOUdBrpWSgjDlRMyGDIaH2AiBAMCEIV1Mig5BKM_DcgaOi4afo7DC3G9dbCB7S0Ltou77dun5ns2vtv0pqv9lN_mE5Y0bXk__57O_z9NEy2G1bPMToEuSxWCUVk1zyCawOoO9zKT00xx2U2H0Tdt-E1dwKOzUx8U_-Dnak59NP-tNZd8W72Ewn9G05YloSrc0-3-MZ208_qjdbnv1Hts0Y4wA_h4l7dOCuy5D7mzCKSMP_AIPQs2Y</recordid><startdate>19860201</startdate><enddate>19860201</enddate><creator>Laperche, Yannick</creator><creator>Bulle, Frédérique</creator><creator>Aissani, Tsouria</creator><creator>Chobert, Marie-Noëlle</creator><creator>Aggerbeck, Martine</creator><creator>Hanoune, Jacques</creator><creator>Guellaen, Georges</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>5PM</scope></search><sort><creationdate>19860201</creationdate><title>Molecular Cloning and Nucleotide Sequence of Rat Kidney γ -glutamyl Transpeptidase cDNA</title><author>Laperche, Yannick ; Bulle, Frédérique ; Aissani, Tsouria ; Chobert, Marie-Noëlle ; Aggerbeck, Martine ; Hanoune, Jacques ; Guellaen, Georges</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4617-1d45308b4aa1e8b776d122a45246d90d5c4eeded9dd4a5106d46782ec3aea14f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>DNA</topic><topic>DNA - analysis</topic><topic>DNA, Recombinant - analysis</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gamma-Glutamyltransferase - genetics</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Kidney - analysis</topic><topic>Kidneys</topic><topic>Liver</topic><topic>Messenger RNA</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular cloning</topic><topic>Nucleotide sequences</topic><topic>Nucleotides</topic><topic>Poly A - genetics</topic><topic>Protein Precursors - genetics</topic><topic>Protein Sorting Signals - genetics</topic><topic>Rats</topic><topic>RNA</topic><topic>RNA, Messenger - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Laperche, Yannick</creatorcontrib><creatorcontrib>Bulle, Frédérique</creatorcontrib><creatorcontrib>Aissani, Tsouria</creatorcontrib><creatorcontrib>Chobert, Marie-Noëlle</creatorcontrib><creatorcontrib>Aggerbeck, Martine</creatorcontrib><creatorcontrib>Hanoune, Jacques</creatorcontrib><creatorcontrib>Guellaen, Georges</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>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>Laperche, Yannick</au><au>Bulle, Frédérique</au><au>Aissani, Tsouria</au><au>Chobert, Marie-Noëlle</au><au>Aggerbeck, Martine</au><au>Hanoune, Jacques</au><au>Guellaen, Georges</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning and Nucleotide Sequence of Rat Kidney γ -glutamyl Transpeptidase cDNA</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1986-02-01</date><risdate>1986</risdate><volume>83</volume><issue>4</issue><spage>937</spage><epage>941</epage><pages>937-941</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have screened a cDNA library (20,000 clones) made from rat kidney poly(A)+ RNA, using an oligonucleotide probe that was a mixture of 14-base DNA oligomers containing all 32 possible sequences coding for residues 32-36 of the γ -glutamyl transpeptidase (EC 2.3.2.2.) heavy chain. We isolated and sequenced two cDNAs corresponding to the mRNA coding for the entire length of the enzyme precursor. The nucleotide sequence that we obtained (2072 bases) reveals an open reading frame of 1707 nucleotides coding for the common precursor of both enzyme subunits. The amino acid sequence begins with the 21 residues located at the NH2-terminal hydrophobic region of the heavy subunit. We show that this sequence, which is not processed, is the only possible signal peptide in the sequence. Five potential N-glycosylation sites are present in the γ -glutamyl transpeptidase sequence. Using one of the two cDNA clones as probe, a 2.2-kilobase sequence was detected by blot analysis in rat kidney and human fetal liver RNA.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2869484</pmid><doi>10.1073/pnas.83.4.937</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Amino acids Animals Base Sequence Biological and medical sciences Biotechnology Cloning, Molecular Complementary DNA DNA DNA - analysis DNA, Recombinant - analysis Enzymes Fundamental and applied biological sciences. Psychology gamma-Glutamyltransferase - genetics Genetic engineering Genetic technics Kidney - analysis Kidneys Liver Messenger RNA Methods. Procedures. Technologies Molecular cloning Nucleotide sequences Nucleotides Poly A - genetics Protein Precursors - genetics Protein Sorting Signals - genetics Rats RNA RNA, Messenger - genetics |
title | Molecular Cloning and Nucleotide Sequence of Rat Kidney γ -glutamyl Transpeptidase cDNA |
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