DNA Polymerase of Bacteriophage T4 is an Autogenous Translational Repressor
In bacteriophage T4 the protein product of gene 43 (gp43) is a multifunctional DNA polymerase that is essential for replication of the phage genome. The protein harbors DNA-binding, deoxyribonucleotide-binding, DNA-synthesizing (polymerase) and 3′-exonucleolytic (editing) activities as well as a cap...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1988-11, Vol.85 (21), p.7942-7946 |
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creator | Andrake, Mark Guild, Nancy Hsu, Tien Gold, Larry Tuerk, Craig Karam, Jim |
description | In bacteriophage T4 the protein product of gene 43 (gp43) is a multifunctional DNA polymerase that is essential for replication of the phage genome. The protein harbors DNA-binding, deoxyribonucleotide-binding, DNA-synthesizing (polymerase) and 3′-exonucleolytic (editing) activities as well as a capacity to interact with several other T4-induced replication enzymes. In addition, the T4 gp43 is a repressor of its own synthesis in vivo. We show here that this protein is an autogenous repressor of translation, and we have localized its RNA-binding sequence (translational operator) to the translation initiation domain of gene 43 mRNA. This mechanism for regulation of T4 DNA polymerase expression underscores the ubiquity of translational repression in the control of T4 DNA replication. Many T4 DNA polymerase accessory proteins and nucleotide biosynthesis enzymes are regulated by the phage-induced translational repressor regA, while the T4 single-stranded DNA-binding protein (T4 gp32) is, like gp43, autogenously regulated at the translational level. |
doi_str_mv | 10.1073/pnas.85.21.7942 |
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The protein harbors DNA-binding, deoxyribonucleotide-binding, DNA-synthesizing (polymerase) and 3′-exonucleolytic (editing) activities as well as a capacity to interact with several other T4-induced replication enzymes. In addition, the T4 gp43 is a repressor of its own synthesis in vivo. We show here that this protein is an autogenous repressor of translation, and we have localized its RNA-binding sequence (translational operator) to the translation initiation domain of gene 43 mRNA. This mechanism for regulation of T4 DNA polymerase expression underscores the ubiquity of translational repression in the control of T4 DNA replication. Many T4 DNA polymerase accessory proteins and nucleotide biosynthesis enzymes are regulated by the phage-induced translational repressor regA, while the T4 single-stranded DNA-binding protein (T4 gp32) is, like gp43, autogenously regulated at the translational level.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.85.21.7942</identifier><identifier>PMID: 3054876</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Bacteriophage T4 ; Bacteriophages ; Base Sequence ; Biological and medical sciences ; DNA ; DNA replication ; DNA-Directed DNA Polymerase - metabolism ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gene expression regulation ; Genes ; Genetics ; Infections ; Messenger RNA ; Microbiology ; Molecular Sequence Data ; Nucleic Acid Conformation ; phage T4 ; Protein Biosynthesis ; Protein Processing, Post-Translational ; Repression ; Repressor Proteins ; RNA ; T-Phages - enzymology ; Transcription Factors ; Virology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1988-11, Vol.85 (21), p.7942-7946</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c467t-ea0c8ab7497868f415414ae4787f231dae5337939fabf83ddaec5805fa08d0cc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/85/21.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/32544$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/32544$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,27933,27934,58026,58259</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6896250$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3054876$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Andrake, Mark</creatorcontrib><creatorcontrib>Guild, Nancy</creatorcontrib><creatorcontrib>Hsu, Tien</creatorcontrib><creatorcontrib>Gold, Larry</creatorcontrib><creatorcontrib>Tuerk, Craig</creatorcontrib><creatorcontrib>Karam, Jim</creatorcontrib><title>DNA Polymerase of Bacteriophage T4 is an Autogenous Translational Repressor</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>In bacteriophage T4 the protein product of gene 43 (gp43) is a multifunctional DNA polymerase that is essential for replication of the phage genome. The protein harbors DNA-binding, deoxyribonucleotide-binding, DNA-synthesizing (polymerase) and 3′-exonucleolytic (editing) activities as well as a capacity to interact with several other T4-induced replication enzymes. In addition, the T4 gp43 is a repressor of its own synthesis in vivo. We show here that this protein is an autogenous repressor of translation, and we have localized its RNA-binding sequence (translational operator) to the translation initiation domain of gene 43 mRNA. This mechanism for regulation of T4 DNA polymerase expression underscores the ubiquity of translational repression in the control of T4 DNA replication. Many T4 DNA polymerase accessory proteins and nucleotide biosynthesis enzymes are regulated by the phage-induced translational repressor regA, while the T4 single-stranded DNA-binding protein (T4 gp32) is, like gp43, autogenously regulated at the translational level.</description><subject>Bacteriophage T4</subject><subject>Bacteriophages</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>DNA</subject><subject>DNA replication</subject><subject>DNA-Directed DNA Polymerase - metabolism</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression regulation</subject><subject>Genes</subject><subject>Genetics</subject><subject>Infections</subject><subject>Messenger RNA</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>phage T4</subject><subject>Protein Biosynthesis</subject><subject>Protein Processing, Post-Translational</subject><subject>Repression</subject><subject>Repressor Proteins</subject><subject>RNA</subject><subject>T-Phages - enzymology</subject><subject>Transcription Factors</subject><subject>Virology</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>eNqFkM9rFDEYhkNR6rb2LAhKDtKeZpufk8xxbWsVi0rZnsO32aROyU7GZAbsf2-GHSte9BTI93zv9_Ig9IqSJSWKn_cd5KWWS0aXqhHsAC0oaWhVi4Y8QwtCmKq0YOIFOsr5gRDSSE0O0SEnUmhVL9Dnyy8r_C2Gx51LkB2OHr8HO7jUxv473Du8FrjNGDq8God477o4ZrxO0OUAQxs7CPjW9cnlHNNL9NxDyO5kfo_R3Yer9cXH6ubr9aeL1U1lRa2GygGxGjZKNErX2gsqBRXghNLKM0634CTnquGNh43XfFs-bGktPRC9JdbyY3S6z-1T_DG6PJhdm60LATpX6hmlZckU7L8glVTVkpACnu9Bm2LOyXnTp3YH6dFQYibPZvJstDSMmslz2XgzR4-bnds-8bPYMn83zyFbCL4Ys21-wmrd1ExOh9_O2JT_e_rXnbN_AsaPIQzu51DI13vyIQ8x_SnEigr-C0l9pi4</recordid><startdate>19881101</startdate><enddate>19881101</enddate><creator>Andrake, Mark</creator><creator>Guild, Nancy</creator><creator>Hsu, Tien</creator><creator>Gold, Larry</creator><creator>Tuerk, Craig</creator><creator>Karam, Jim</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>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19881101</creationdate><title>DNA Polymerase of Bacteriophage T4 is an Autogenous Translational Repressor</title><author>Andrake, Mark ; Guild, Nancy ; Hsu, Tien ; Gold, Larry ; Tuerk, Craig ; Karam, Jim</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c467t-ea0c8ab7497868f415414ae4787f231dae5337939fabf83ddaec5805fa08d0cc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Bacteriophage T4</topic><topic>Bacteriophages</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>DNA</topic><topic>DNA replication</topic><topic>DNA-Directed DNA Polymerase - metabolism</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression regulation</topic><topic>Genes</topic><topic>Genetics</topic><topic>Infections</topic><topic>Messenger RNA</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>phage T4</topic><topic>Protein Biosynthesis</topic><topic>Protein Processing, Post-Translational</topic><topic>Repression</topic><topic>Repressor Proteins</topic><topic>RNA</topic><topic>T-Phages - enzymology</topic><topic>Transcription Factors</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Andrake, Mark</creatorcontrib><creatorcontrib>Guild, Nancy</creatorcontrib><creatorcontrib>Hsu, Tien</creatorcontrib><creatorcontrib>Gold, Larry</creatorcontrib><creatorcontrib>Tuerk, Craig</creatorcontrib><creatorcontrib>Karam, Jim</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>Virology and AIDS Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Andrake, Mark</au><au>Guild, Nancy</au><au>Hsu, Tien</au><au>Gold, Larry</au><au>Tuerk, Craig</au><au>Karam, Jim</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DNA Polymerase of Bacteriophage T4 is an Autogenous Translational Repressor</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1988-11-01</date><risdate>1988</risdate><volume>85</volume><issue>21</issue><spage>7942</spage><epage>7946</epage><pages>7942-7946</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>In bacteriophage T4 the protein product of gene 43 (gp43) is a multifunctional DNA polymerase that is essential for replication of the phage genome. The protein harbors DNA-binding, deoxyribonucleotide-binding, DNA-synthesizing (polymerase) and 3′-exonucleolytic (editing) activities as well as a capacity to interact with several other T4-induced replication enzymes. In addition, the T4 gp43 is a repressor of its own synthesis in vivo. We show here that this protein is an autogenous repressor of translation, and we have localized its RNA-binding sequence (translational operator) to the translation initiation domain of gene 43 mRNA. This mechanism for regulation of T4 DNA polymerase expression underscores the ubiquity of translational repression in the control of T4 DNA replication. Many T4 DNA polymerase accessory proteins and nucleotide biosynthesis enzymes are regulated by the phage-induced translational repressor regA, while the T4 single-stranded DNA-binding protein (T4 gp32) is, like gp43, autogenously regulated at the translational level.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3054876</pmid><doi>10.1073/pnas.85.21.7942</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Bacteriophage T4 Bacteriophages Base Sequence Biological and medical sciences DNA DNA replication DNA-Directed DNA Polymerase - metabolism Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene expression regulation Genes Genetics Infections Messenger RNA Microbiology Molecular Sequence Data Nucleic Acid Conformation phage T4 Protein Biosynthesis Protein Processing, Post-Translational Repression Repressor Proteins RNA T-Phages - enzymology Transcription Factors Virology |
title | DNA Polymerase of Bacteriophage T4 is an Autogenous Translational Repressor |
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