Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA
The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV‐sensitive mutants. The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐19...
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description | The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV‐sensitive mutants. The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2‐197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5′ end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2‐197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2‐197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two‐hybrid screen and found Rad51 as a candidate. Rec2‐197 and Rad51 appear to interact to a similar degree. |
doi_str_mv | 10.1046/j.1365-2958.2001.02490.x |
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The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2‐197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5′ end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2‐197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2‐197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two‐hybrid screen and found Rad51 as a candidate. Rec2‐197 and Rad51 appear to interact to a similar degree.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.2001.02490.x</identifier><identifier>PMID: 11442839</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science, Ltd</publisher><subject>Amino Acid Sequence ; Binding Sites ; Chromosome Segregation ; Diploidy ; DNA Repair - drug effects ; DNA Repair - genetics ; DNA Repair - radiation effects ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Homozygote ; Meiosis ; Methyl Methanesulfonate - pharmacology ; Molecular Sequence Data ; Mutagens - pharmacology ; Mutation ; Protein Structure, Tertiary ; Rad51 protein ; REC2 gene ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Recombination, Genetic ; Spores, Fungal - physiology ; Two-Hybrid System Techniques ; Ultraviolet Rays ; Ustilago - drug effects ; Ustilago - physiology ; Ustilago - radiation effects ; Ustilago maydis ; Yeasts - genetics</subject><ispartof>Molecular microbiology, 2001-06, Vol.40 (6), p.1415-1426</ispartof><rights>Copyright Blackwell Scientific Publications Ltd. Jun 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4730-edec81bde339d5e7890162df68c53a05fc8c41aada1ebe6f2d3973034f186b043</citedby><cites>FETCH-LOGICAL-c4730-edec81bde339d5e7890162df68c53a05fc8c41aada1ebe6f2d3973034f186b043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-2958.2001.02490.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-2958.2001.02490.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11442839$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kojic, Milorad</creatorcontrib><creatorcontrib>Thompson, Chad W.</creatorcontrib><creatorcontrib>Holloman, William K.</creatorcontrib><title>Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV‐sensitive mutants. The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2‐197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5′ end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2‐197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2‐197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two‐hybrid screen and found Rad51 as a candidate. Rec2‐197 and Rad51 appear to interact to a similar degree.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Chromosome Segregation</subject><subject>Diploidy</subject><subject>DNA Repair - drug effects</subject><subject>DNA Repair - genetics</subject><subject>DNA Repair - radiation effects</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Homozygote</subject><subject>Meiosis</subject><subject>Methyl Methanesulfonate - pharmacology</subject><subject>Molecular Sequence Data</subject><subject>Mutagens - pharmacology</subject><subject>Mutation</subject><subject>Protein Structure, Tertiary</subject><subject>Rad51 protein</subject><subject>REC2 gene</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Recombination, Genetic</subject><subject>Spores, Fungal - physiology</subject><subject>Two-Hybrid System Techniques</subject><subject>Ultraviolet Rays</subject><subject>Ustilago - drug effects</subject><subject>Ustilago - physiology</subject><subject>Ustilago - radiation effects</subject><subject>Ustilago maydis</subject><subject>Yeasts - genetics</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtv1DAUhS0EokPhLyCLBbsEP1N7waKaFqjUgoSoxM5y4pvBoyQOtiM64s_jMCOQWLE6fnzn3CsdhDAlNSWiebOvKW9kxbRUNSOE1oQJTeqHR2jz5-Mx2hAtScUV-3qGnqW0LyAnDX-KzigVgimuN-jnlU9xmbMPU8Khx_kb4PuU_WB3AY_24HzCn6-3DO9gAuwdTNn3B2zxHEMGP2EXRlvEj3OI2U4Zr28-Qpf9tMNFw9j6ya4D7FDus_VxHXT18fI5etLbIcGLk56j-3fXX7YfqttP72-2l7dVJy44qcBBp2jrgHPtJFwoTWjDXN-oTnJLZN-pTlBrnaXQQtMzx3XxcdFT1bRE8HP0-phbdv6-QMpm9KmDYbAThCUZqiiTsmEFfPUPuA9LLHsXRjdCa8JkgdQR6mJIKUJv5uhHGw-GErO2Y_ZmLcGsJZi1HfO7HfNQrC9P-Us7gvtrPNVRgLdH4Icf4PDfwebu7mY98V8k9Z8G</recordid><startdate>200106</startdate><enddate>200106</enddate><creator>Kojic, Milorad</creator><creator>Thompson, Chad W.</creator><creator>Holloman, William K.</creator><general>Blackwell Science, Ltd</general><general>Blackwell Publishing Ltd</general><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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200106</creationdate><title>Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA</title><author>Kojic, Milorad ; Thompson, Chad W. ; Holloman, William K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4730-edec81bde339d5e7890162df68c53a05fc8c41aada1ebe6f2d3973034f186b043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Chromosome Segregation</topic><topic>Diploidy</topic><topic>DNA Repair - drug effects</topic><topic>DNA Repair - genetics</topic><topic>DNA Repair - radiation effects</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Homozygote</topic><topic>Meiosis</topic><topic>Methyl Methanesulfonate - pharmacology</topic><topic>Molecular Sequence Data</topic><topic>Mutagens - pharmacology</topic><topic>Mutation</topic><topic>Protein Structure, Tertiary</topic><topic>Rad51 protein</topic><topic>REC2 gene</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Recombination, Genetic</topic><topic>Spores, Fungal - physiology</topic><topic>Two-Hybrid System Techniques</topic><topic>Ultraviolet Rays</topic><topic>Ustilago - drug effects</topic><topic>Ustilago - physiology</topic><topic>Ustilago - radiation effects</topic><topic>Ustilago maydis</topic><topic>Yeasts - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kojic, Milorad</creatorcontrib><creatorcontrib>Thompson, Chad W.</creatorcontrib><creatorcontrib>Holloman, William K.</creatorcontrib><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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kojic, Milorad</au><au>Thompson, Chad W.</au><au>Holloman, William K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2001-06</date><risdate>2001</risdate><volume>40</volume><issue>6</issue><spage>1415</spage><epage>1426</epage><pages>1415-1426</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV‐sensitive mutants. The original isolate, rec2‐1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2‐197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2‐197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5′ end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2‐197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2‐197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two‐hybrid screen and found Rad51 as a candidate. Rec2‐197 and Rad51 appear to interact to a similar degree.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science, Ltd</pub><pmid>11442839</pmid><doi>10.1046/j.1365-2958.2001.02490.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Binding Sites Chromosome Segregation Diploidy DNA Repair - drug effects DNA Repair - genetics DNA Repair - radiation effects Fungal Proteins - genetics Fungal Proteins - metabolism Homozygote Meiosis Methyl Methanesulfonate - pharmacology Molecular Sequence Data Mutagens - pharmacology Mutation Protein Structure, Tertiary Rad51 protein REC2 gene Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Recombination, Genetic Spores, Fungal - physiology Two-Hybrid System Techniques Ultraviolet Rays Ustilago - drug effects Ustilago - physiology Ustilago - radiation effects Ustilago maydis Yeasts - genetics |
title | Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA |
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