Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine
The authors have isolated a cdNA coding the human enzyme from a kidney library in lambda gt10 by cross-hybridization with a bovine cDNA; 24 of 5300 clones hybridized with the probe. The active site selenocysteine residue (-CH sub(2) SeH) at position 47 (i.e. SeC) is encoded by the nonsense codon, TG...
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| Veröffentlicht in: | Nucleic acids research 1987-07, Vol.15 (13), p.5484-5484 |
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| container_title | Nucleic acids research |
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| creator | MULLENBACH, G. T TABRIZI, A IRVINE, B. D BELL, G. I HALLEWELL, R. A |
| description | The authors have isolated a cdNA coding the human enzyme from a kidney library in lambda gt10 by cross-hybridization with a bovine cDNA; 24 of 5300 clones hybridized with the probe. The active site selenocysteine residue (-CH sub(2) SeH) at position 47 (i.e. SeC) is encoded by the nonsense codon, TGA, as is similarly observed in the mouse gene. Interestingly evidence suggests that the selenium atom is incorporated cotranslationally rather than via a posttranslational modification step. This clone possesses 5 bp of the 5'-untranslated region, the 603 bp coding region, 223 bp to the 3'-untranslated region and a canonical polyadenylation signal, AATAAA, upstream of the polyA tract. The amino acid sequence reveals the protein possesses approximately 87% and 85% homology with preprocessed bovine and mouse enzymes, respectively. |
| doi_str_mv | 10.1093/nar/15.13.5484 |
| format | Article |
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T ; TABRIZI, A ; IRVINE, B. D ; BELL, G. I ; HALLEWELL, R. A</creator><creatorcontrib>MULLENBACH, G. T ; TABRIZI, A ; IRVINE, B. D ; BELL, G. I ; HALLEWELL, R. A</creatorcontrib><description>The authors have isolated a cdNA coding the human enzyme from a kidney library in lambda gt10 by cross-hybridization with a bovine cDNA; 24 of 5300 clones hybridized with the probe. The active site selenocysteine residue (-CH sub(2) SeH) at position 47 (i.e. SeC) is encoded by the nonsense codon, TGA, as is similarly observed in the mouse gene. Interestingly evidence suggests that the selenium atom is incorporated cotranslationally rather than via a posttranslational modification step. This clone possesses 5 bp of the 5'-untranslated region, the 603 bp coding region, 223 bp to the 3'-untranslated region and a canonical polyadenylation signal, AATAAA, upstream of the polyA tract. 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T</creatorcontrib><creatorcontrib>TABRIZI, A</creatorcontrib><creatorcontrib>IRVINE, B. D</creatorcontrib><creatorcontrib>BELL, G. I</creatorcontrib><creatorcontrib>HALLEWELL, R. A</creatorcontrib><title>Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>The authors have isolated a cdNA coding the human enzyme from a kidney library in lambda gt10 by cross-hybridization with a bovine cDNA; 24 of 5300 clones hybridized with the probe. The active site selenocysteine residue (-CH sub(2) SeH) at position 47 (i.e. SeC) is encoded by the nonsense codon, TGA, as is similarly observed in the mouse gene. Interestingly evidence suggests that the selenium atom is incorporated cotranslationally rather than via a posttranslational modification step. This clone possesses 5 bp of the 5'-untranslated region, the 603 bp coding region, 223 bp to the 3'-untranslated region and a canonical polyadenylation signal, AATAAA, upstream of the polyA tract. The amino acid sequence reveals the protein possesses approximately 87% and 85% homology with preprocessed bovine and mouse enzymes, respectively.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>cDNA</subject><subject>Cysteine - analogs & derivatives</subject><subject>Cysteine - analysis</subject><subject>DNA - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Genes. Genome</subject><subject>glutathione peroxidase</subject><subject>Glutathione Peroxidase - genetics</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>nucleotide sequence</subject><subject>Selenium - analysis</subject><subject>Selenocysteine</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkTFvHCEQhZGVyDk7bt1ZoojS7ZlZYFmKFCcndiJZSZHrEcfO3mHtwgV2LfvfB8unU1JZQlC874148wi5BLYEpvl1sOka5BL4UopWnJAF8KauhG7qd2TBOJMVMNF-IGc5PzAGAqQ4Jae1lrJu1YI8_MY_MwaHNPbUUvf154q62PmwpX1MdDePNtDtME922vkYkO4xxSff2YyFC71PY6bruxUtM2KHmVo3-Uek2U_lwgFDdM95Qh_wI3nf2yHjxeE9J-vbb-ub79X9r7sfN6v7yknFpqoGcE3dKF0iuLYTPddYEjTYl2BKdHZjmew2nW55LWUvm41VClBZoRQDyc_Jl9ex-3kzYucwTMkOZp_8aNOzidab_5Xgd2YbH03ZlVa6-D8f_CmW1eTJjD47HAYbMM7ZKNUwXrfwJgiaC9Hq-m1QtApAsQIuX0GXYs4J--OvgZmXtk1p24A0wM1L28Vw9W_WI36ot-ifDrrNzg59ssH5fMSUUMDL-QtHhrOq</recordid><startdate>19870710</startdate><enddate>19870710</enddate><creator>MULLENBACH, G. 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A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c570t-211c62679962c8d4f39e0486ef36274daba05dbd983255f56ba771e7a4770153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>cDNA</topic><topic>Cysteine - analogs & derivatives</topic><topic>Cysteine - analysis</topic><topic>DNA - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes</topic><topic>Genes. Genome</topic><topic>glutathione peroxidase</topic><topic>Glutathione Peroxidase - genetics</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>nucleotide sequence</topic><topic>Selenium - analysis</topic><topic>Selenocysteine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MULLENBACH, G. T</creatorcontrib><creatorcontrib>TABRIZI, A</creatorcontrib><creatorcontrib>IRVINE, B. D</creatorcontrib><creatorcontrib>BELL, G. I</creatorcontrib><creatorcontrib>HALLEWELL, R. A</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>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MULLENBACH, G. T</au><au>TABRIZI, A</au><au>IRVINE, B. D</au><au>BELL, G. I</au><au>HALLEWELL, R. A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1987-07-10</date><risdate>1987</risdate><volume>15</volume><issue>13</issue><spage>5484</spage><epage>5484</epage><pages>5484-5484</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><coden>NARHAD</coden><abstract>The authors have isolated a cdNA coding the human enzyme from a kidney library in lambda gt10 by cross-hybridization with a bovine cDNA; 24 of 5300 clones hybridized with the probe. The active site selenocysteine residue (-CH sub(2) SeH) at position 47 (i.e. SeC) is encoded by the nonsense codon, TGA, as is similarly observed in the mouse gene. Interestingly evidence suggests that the selenium atom is incorporated cotranslationally rather than via a posttranslational modification step. This clone possesses 5 bp of the 5'-untranslated region, the 603 bp coding region, 223 bp to the 3'-untranslated region and a canonical polyadenylation signal, AATAAA, upstream of the polyA tract. The amino acid sequence reveals the protein possesses approximately 87% and 85% homology with preprocessed bovine and mouse enzymes, respectively.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>2955287</pmid><doi>10.1093/nar/15.13.5484</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nucleic acids research, 1987-07, Vol.15 (13), p.5484-5484 |
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| source | Oxford University Press Journals Digital Archive legacy; MEDLINE; PubMed Central |
| subjects | Amino Acid Sequence Base Sequence Binding Sites Biological and medical sciences cDNA Cysteine - analogs & derivatives Cysteine - analysis DNA - analysis Fundamental and applied biological sciences. Psychology Genes Genes. Genome glutathione peroxidase Glutathione Peroxidase - genetics Humans Molecular and cellular biology Molecular genetics nucleotide sequence Selenium - analysis Selenocysteine |
| title | Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine |
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