Molecular cloning of human uracil‐DNA glycosylase, a highly conserved DNA repair enzyme
Uracil‐DNA glycosylase is the DNA repair enzyme responsible for the removal of uracil from DNA, and it is present in all organisms investigated. Here we report on the cloning and sequencing of a cDNA encoding the human uracil‐DNA glycosylase. The sequences of uracil‐DNA glycosylases from yeast, Esch...
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| Veröffentlicht in: | The EMBO journal 1989-10, Vol.8 (10), p.3121-3125 |
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| creator | Olsen, L.C. Aasland, R. Wittwer, C.U. Krokan, H.E. Helland, D.E. |
| description | Uracil‐DNA glycosylase is the DNA repair enzyme responsible for the removal of uracil from DNA, and it is present in all organisms investigated. Here we report on the cloning and sequencing of a cDNA encoding the human uracil‐DNA glycosylase. The sequences of uracil‐DNA glycosylases from yeast, Escherichia coli, herpes simplex virus type 1 and 2, and homologous genes from varicella‐zoster and Epstein‐Barr viruses are known. It is shown in this report that the predicted amino acid sequence of the human uracil‐DNA glycosylase shows a striking similarity to the other uracil‐DNA glycosylases, ranging from 40.3 to 55.7% identical residues. The proteins of human and bacterial origin were unexpectedly found to be most closely related, 73.3% similarity when conservative amino acid substitutions were included. The similarity between the different uracil‐DNA glycosylase genes is confined to several discrete boxes. These findings strongly indicate that uracil‐DNA glycosylases from phylogenetically distant species are highly conserved. |
| doi_str_mv | 10.1002/j.1460-2075.1989.tb08464.x |
| format | Article |
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Here we report on the cloning and sequencing of a cDNA encoding the human uracil‐DNA glycosylase. The sequences of uracil‐DNA glycosylases from yeast, Escherichia coli, herpes simplex virus type 1 and 2, and homologous genes from varicella‐zoster and Epstein‐Barr viruses are known. It is shown in this report that the predicted amino acid sequence of the human uracil‐DNA glycosylase shows a striking similarity to the other uracil‐DNA glycosylases, ranging from 40.3 to 55.7% identical residues. The proteins of human and bacterial origin were unexpectedly found to be most closely related, 73.3% similarity when conservative amino acid substitutions were included. The similarity between the different uracil‐DNA glycosylase genes is confined to several discrete boxes. These findings strongly indicate that uracil‐DNA glycosylases from phylogenetically distant species are highly conserved.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1989.tb08464.x</identifier><identifier>PMID: 2555154</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Amino Acid Sequence ; Base Sequence ; Biological and medical sciences ; Blotting, Northern ; Blotting, Southern ; Cloning, Molecular ; DNA Glycosylases ; DNA Ligases - genetics ; Escherichia coli - genetics ; Female ; Fundamental and applied biological sciences. Psychology ; Genes. Genome ; Herpesvirus 3, Human - genetics ; Herpesvirus 4, Human - genetics ; Humans ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; N-Glycosyl Hydrolases - genetics ; Polynucleotide Ligases - genetics ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Simplexvirus - genetics ; Uracil-DNA Glycosidase ; Yeasts - genetics</subject><ispartof>The EMBO journal, 1989-10, Vol.8 (10), p.3121-3125</ispartof><rights>1989 European Molecular Biology Organization</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5734-d2043dc6c302ed7a401df8a8bbcf72823ce89d5e1bd08ba0de93725beef284b63</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC401392/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC401392/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6742010$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2555154$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olsen, L.C.</creatorcontrib><creatorcontrib>Aasland, R.</creatorcontrib><creatorcontrib>Wittwer, C.U.</creatorcontrib><creatorcontrib>Krokan, H.E.</creatorcontrib><creatorcontrib>Helland, D.E.</creatorcontrib><title>Molecular cloning of human uracil‐DNA glycosylase, a highly conserved DNA repair enzyme</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Uracil‐DNA glycosylase is the DNA repair enzyme responsible for the removal of uracil from DNA, and it is present in all organisms investigated. Here we report on the cloning and sequencing of a cDNA encoding the human uracil‐DNA glycosylase. The sequences of uracil‐DNA glycosylases from yeast, Escherichia coli, herpes simplex virus type 1 and 2, and homologous genes from varicella‐zoster and Epstein‐Barr viruses are known. It is shown in this report that the predicted amino acid sequence of the human uracil‐DNA glycosylase shows a striking similarity to the other uracil‐DNA glycosylases, ranging from 40.3 to 55.7% identical residues. The proteins of human and bacterial origin were unexpectedly found to be most closely related, 73.3% similarity when conservative amino acid substitutions were included. The similarity between the different uracil‐DNA glycosylase genes is confined to several discrete boxes. These findings strongly indicate that uracil‐DNA glycosylases from phylogenetically distant species are highly conserved.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Blotting, Southern</subject><subject>Cloning, Molecular</subject><subject>DNA Glycosylases</subject><subject>DNA Ligases - genetics</subject><subject>Escherichia coli - genetics</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes. Genome</subject><subject>Herpesvirus 3, Human - genetics</subject><subject>Herpesvirus 4, Human - genetics</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>N-Glycosyl Hydrolases - genetics</subject><subject>Polynucleotide Ligases - genetics</subject><subject>Restriction Mapping</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Simplexvirus - genetics</subject><subject>Uracil-DNA Glycosidase</subject><subject>Yeasts - genetics</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS1EVYbCIyBZCLEiwX9JHCQWQ2kLqIUNLFhZjnMz45ETD_akNKx4hD5jn6QJE41gycpXOt_xvToHoeeUpJQQ9nqTUpGThJEiS2kpy3RXESlykd48QIuD9BAtCMtpIqgsH6HHMW4IIZks6DE6ZlmW0Uws0Pcr78D0TgdsnO9st8K-weu-1R3ugzbW3f2-ff95iVduMD4OTkd4hTVe29XaDdj4LkK4hhpPTICttgFD92to4Qk6arSL8HR-T9C387Ovpx-Syy8XH0-Xl4nJCi6SmhHBa5MbThjUhRaE1o3UsqpMUzDJuAFZ1hnQqiay0qSGkhcsqwAaJkWV8xP0dv_vtq9aqA10u6Cd2gbb6jAor636V-nsWq38tRo38ZKN_pezP_gfPcSdam004JzuwPdRFSXnY-pyBN_sQRN8jAGaww5K1NSL2qgpfDWFr6Ze1NyLuhnNz_6-8mCdixj1F7Ouo9GuCbozNh6wvBCMUDJiyz320zoY_uMAdXb17tOfmd8D4WKuCg</recordid><startdate>198910</startdate><enddate>198910</enddate><creator>Olsen, L.C.</creator><creator>Aasland, R.</creator><creator>Wittwer, C.U.</creator><creator>Krokan, H.E.</creator><creator>Helland, D.E.</creator><general>Nature Publishing Group</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>198910</creationdate><title>Molecular cloning of human uracil‐DNA glycosylase, a highly conserved DNA repair enzyme</title><author>Olsen, L.C. ; Aasland, R. ; Wittwer, C.U. ; Krokan, H.E. ; Helland, D.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5734-d2043dc6c302ed7a401df8a8bbcf72823ce89d5e1bd08ba0de93725beef284b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Blotting, Southern</topic><topic>Cloning, Molecular</topic><topic>DNA Glycosylases</topic><topic>DNA Ligases - genetics</topic><topic>Escherichia coli - genetics</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes. Genome</topic><topic>Herpesvirus 3, Human - genetics</topic><topic>Herpesvirus 4, Human - genetics</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>N-Glycosyl Hydrolases - genetics</topic><topic>Polynucleotide Ligases - genetics</topic><topic>Restriction Mapping</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Simplexvirus - genetics</topic><topic>Uracil-DNA Glycosidase</topic><topic>Yeasts - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olsen, L.C.</creatorcontrib><creatorcontrib>Aasland, R.</creatorcontrib><creatorcontrib>Wittwer, C.U.</creatorcontrib><creatorcontrib>Krokan, H.E.</creatorcontrib><creatorcontrib>Helland, D.E.</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>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Olsen, L.C.</au><au>Aasland, R.</au><au>Wittwer, C.U.</au><au>Krokan, H.E.</au><au>Helland, D.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning of human uracil‐DNA glycosylase, a highly conserved DNA repair enzyme</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1989-10</date><risdate>1989</risdate><volume>8</volume><issue>10</issue><spage>3121</spage><epage>3125</epage><pages>3121-3125</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Uracil‐DNA glycosylase is the DNA repair enzyme responsible for the removal of uracil from DNA, and it is present in all organisms investigated. Here we report on the cloning and sequencing of a cDNA encoding the human uracil‐DNA glycosylase. The sequences of uracil‐DNA glycosylases from yeast, Escherichia coli, herpes simplex virus type 1 and 2, and homologous genes from varicella‐zoster and Epstein‐Barr viruses are known. It is shown in this report that the predicted amino acid sequence of the human uracil‐DNA glycosylase shows a striking similarity to the other uracil‐DNA glycosylases, ranging from 40.3 to 55.7% identical residues. The proteins of human and bacterial origin were unexpectedly found to be most closely related, 73.3% similarity when conservative amino acid substitutions were included. The similarity between the different uracil‐DNA glycosylase genes is confined to several discrete boxes. These findings strongly indicate that uracil‐DNA glycosylases from phylogenetically distant species are highly conserved.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>2555154</pmid><doi>10.1002/j.1460-2075.1989.tb08464.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Base Sequence Biological and medical sciences Blotting, Northern Blotting, Southern Cloning, Molecular DNA Glycosylases DNA Ligases - genetics Escherichia coli - genetics Female Fundamental and applied biological sciences. Psychology Genes. Genome Herpesvirus 3, Human - genetics Herpesvirus 4, Human - genetics Humans Molecular and cellular biology Molecular genetics Molecular Sequence Data N-Glycosyl Hydrolases - genetics Polynucleotide Ligases - genetics Restriction Mapping Sequence Homology, Nucleic Acid Simplexvirus - genetics Uracil-DNA Glycosidase Yeasts - genetics |
| title | Molecular cloning of human uracil‐DNA glycosylase, a highly conserved DNA repair enzyme |
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