Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation–π interactions
Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O ⁶-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-11, Vol.109 (46), p.18755-18760 |
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| creator | Wilkinson, Oliver J Latypov, Vitaly Tubbs, Julie L Millington, Christopher L Morita, Rihito Blackburn, Hannah Marriott, Andrew McGown, Gail Thorncroft, Mary Watson, Amanda J Connolly, Bernard A Grasby, Jane A Masui, Ryoji Hunter, Christopher A Tainer, John A Margison, Geoffrey P Williams, David M |
| description | Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O ⁶-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O ⁶-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O ⁶-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O ⁶-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O ⁶-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O ⁶-alkylguanines critical for NER recognition. |
| doi_str_mv | 10.1073/pnas.1209451109 |
| format | Article |
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We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O ⁶-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O ⁶-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O ⁶-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O ⁶-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O ⁶-alkylguanines critical for NER recognition.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1209451109</identifier><identifier>PMID: 23112169</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>adverse effects ; Alkyl and Aryl Transferases - chemistry ; Alkyl and Aryl Transferases - genetics ; Alkyl and Aryl Transferases - metabolism ; Alkylation ; Amino Acid Substitution ; Atomic interactions ; Atoms ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biological Sciences ; Crystal structure ; Crystallography, X-Ray ; DNA ; DNA damage ; DNA repair ; DNA Repair - physiology ; guanine ; Guanine - chemistry ; Guanine - metabolism ; Hydrogen ; Lesions ; mechanics ; Molecular interactions ; mutants ; Mutation, Missense ; oligodeoxyribonucleotides ; Oligodeoxyribonucleotides - chemistry ; Oligodeoxyribonucleotides - genetics ; Oligodeoxyribonucleotides - metabolism ; Physical Sciences ; Protein Binding ; Protein Structure, Tertiary ; proteins ; Purines ; Schizosaccharomyces - enzymology ; Schizosaccharomyces - genetics ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Thermus thermophilus ; Thermus thermophilus - enzymology ; toxicity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (46), p.18755-18760</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c497t-b213dae167cdc718a73d970241aff2ee3d6df58f6fc14c1c80f6e87e876c2e0d3</citedby><cites>FETCH-LOGICAL-c497t-b213dae167cdc718a73d970241aff2ee3d6df58f6fc14c1c80f6e87e876c2e0d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/46.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41830098$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41830098$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23112169$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilkinson, Oliver J</creatorcontrib><creatorcontrib>Latypov, Vitaly</creatorcontrib><creatorcontrib>Tubbs, Julie L</creatorcontrib><creatorcontrib>Millington, Christopher L</creatorcontrib><creatorcontrib>Morita, Rihito</creatorcontrib><creatorcontrib>Blackburn, Hannah</creatorcontrib><creatorcontrib>Marriott, Andrew</creatorcontrib><creatorcontrib>McGown, Gail</creatorcontrib><creatorcontrib>Thorncroft, Mary</creatorcontrib><creatorcontrib>Watson, Amanda J</creatorcontrib><creatorcontrib>Connolly, Bernard A</creatorcontrib><creatorcontrib>Grasby, Jane A</creatorcontrib><creatorcontrib>Masui, Ryoji</creatorcontrib><creatorcontrib>Hunter, Christopher A</creatorcontrib><creatorcontrib>Tainer, John A</creatorcontrib><creatorcontrib>Margison, Geoffrey P</creatorcontrib><creatorcontrib>Williams, David M</creatorcontrib><title>Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation–π interactions</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O ⁶-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O ⁶-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O ⁶-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O ⁶-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O ⁶-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O ⁶-alkylguanines critical for NER recognition.</description><subject>adverse effects</subject><subject>Alkyl and Aryl Transferases - chemistry</subject><subject>Alkyl and Aryl Transferases - genetics</subject><subject>Alkyl and Aryl Transferases - metabolism</subject><subject>Alkylation</subject><subject>Amino Acid Substitution</subject><subject>Atomic interactions</subject><subject>Atoms</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological Sciences</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>DNA</subject><subject>DNA damage</subject><subject>DNA repair</subject><subject>DNA Repair - physiology</subject><subject>guanine</subject><subject>Guanine - chemistry</subject><subject>Guanine - metabolism</subject><subject>Hydrogen</subject><subject>Lesions</subject><subject>mechanics</subject><subject>Molecular interactions</subject><subject>mutants</subject><subject>Mutation, Missense</subject><subject>oligodeoxyribonucleotides</subject><subject>Oligodeoxyribonucleotides - chemistry</subject><subject>Oligodeoxyribonucleotides - genetics</subject><subject>Oligodeoxyribonucleotides - metabolism</subject><subject>Physical Sciences</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>proteins</subject><subject>Purines</subject><subject>Schizosaccharomyces - enzymology</subject><subject>Schizosaccharomyces - genetics</subject><subject>Schizosaccharomyces pombe</subject><subject>Schizosaccharomyces pombe Proteins - chemistry</subject><subject>Schizosaccharomyces pombe Proteins - genetics</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>Thermus thermophilus</subject><subject>Thermus thermophilus - enzymology</subject><subject>toxicity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkc9u1DAQxi0EokvhzAnwsRzSzsSJ41yQVqX8kSo4QM-W69hbt1l7sR2k3voOPFjfgSfB0S5bkCxbmu8333j0EfIS4RihYycbr9Ix1tA3LSL0j8ii3FjxpofHZAFQd5Vo6uaAPEvpGgD6VsBTclAzxBp5vyBpOd7cjjkqn6yJKplqdDeGbmLIxnl6tMwjvqWDS9n51eTSlUlUzS0qm4GuJuWdLyUbIn3_ZUmj2SgX6ZQKTbXKLvjfd7_u76jzudjruZCekydWjcm82L2H5OLD2ffTT9X514-fT5fnlW76LleXNbJBGeSdHnSHQnVs6DuoG1TW1sawgQ-2FZZbjY1GLcByI7pyuK4NDOyQvNv6bqbLtRm08WXPUW6iW6t4K4Ny8n_Fuyu5Cj8la4Ehx2JwtDOI4cdkUpZrl7QZR-VNmJJEAQwEsrYp6MkW1TGkFI3dj0GQc1Ryjko-RFU6Xv_7uz3_N5sC0B0wdz7Y9bLhZXTXtgV5tUWuUw5xzzQoWMlaFP3NVrcqSLWKLsmLbzUgB0BWdgT2B_bFsdc</recordid><startdate>20121113</startdate><enddate>20121113</enddate><creator>Wilkinson, Oliver J</creator><creator>Latypov, Vitaly</creator><creator>Tubbs, Julie L</creator><creator>Millington, Christopher L</creator><creator>Morita, Rihito</creator><creator>Blackburn, Hannah</creator><creator>Marriott, Andrew</creator><creator>McGown, Gail</creator><creator>Thorncroft, Mary</creator><creator>Watson, Amanda J</creator><creator>Connolly, Bernard A</creator><creator>Grasby, Jane A</creator><creator>Masui, Ryoji</creator><creator>Hunter, Christopher A</creator><creator>Tainer, John A</creator><creator>Margison, Geoffrey P</creator><creator>Williams, David M</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20121113</creationdate><title>Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation–π interactions</title><author>Wilkinson, Oliver J ; Latypov, Vitaly ; Tubbs, Julie L ; Millington, Christopher L ; Morita, Rihito ; Blackburn, Hannah ; Marriott, Andrew ; McGown, Gail ; Thorncroft, Mary ; Watson, Amanda J ; Connolly, Bernard A ; Grasby, Jane A ; Masui, Ryoji ; Hunter, Christopher A ; Tainer, John A ; Margison, Geoffrey P ; Williams, David M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c497t-b213dae167cdc718a73d970241aff2ee3d6df58f6fc14c1c80f6e87e876c2e0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>adverse effects</topic><topic>Alkyl and Aryl Transferases - chemistry</topic><topic>Alkyl and Aryl Transferases - genetics</topic><topic>Alkyl and Aryl Transferases - metabolism</topic><topic>Alkylation</topic><topic>Amino Acid Substitution</topic><topic>Atomic interactions</topic><topic>Atoms</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biological Sciences</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>DNA</topic><topic>DNA damage</topic><topic>DNA repair</topic><topic>DNA Repair - physiology</topic><topic>guanine</topic><topic>Guanine - chemistry</topic><topic>Guanine - metabolism</topic><topic>Hydrogen</topic><topic>Lesions</topic><topic>mechanics</topic><topic>Molecular interactions</topic><topic>mutants</topic><topic>Mutation, Missense</topic><topic>oligodeoxyribonucleotides</topic><topic>Oligodeoxyribonucleotides - chemistry</topic><topic>Oligodeoxyribonucleotides - genetics</topic><topic>Oligodeoxyribonucleotides - metabolism</topic><topic>Physical Sciences</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>proteins</topic><topic>Purines</topic><topic>Schizosaccharomyces - enzymology</topic><topic>Schizosaccharomyces - genetics</topic><topic>Schizosaccharomyces pombe</topic><topic>Schizosaccharomyces pombe Proteins - chemistry</topic><topic>Schizosaccharomyces pombe Proteins - genetics</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>Thermus thermophilus</topic><topic>Thermus thermophilus - enzymology</topic><topic>toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilkinson, Oliver J</creatorcontrib><creatorcontrib>Latypov, Vitaly</creatorcontrib><creatorcontrib>Tubbs, Julie L</creatorcontrib><creatorcontrib>Millington, Christopher L</creatorcontrib><creatorcontrib>Morita, Rihito</creatorcontrib><creatorcontrib>Blackburn, Hannah</creatorcontrib><creatorcontrib>Marriott, Andrew</creatorcontrib><creatorcontrib>McGown, Gail</creatorcontrib><creatorcontrib>Thorncroft, Mary</creatorcontrib><creatorcontrib>Watson, Amanda J</creatorcontrib><creatorcontrib>Connolly, Bernard A</creatorcontrib><creatorcontrib>Grasby, Jane A</creatorcontrib><creatorcontrib>Masui, Ryoji</creatorcontrib><creatorcontrib>Hunter, Christopher A</creatorcontrib><creatorcontrib>Tainer, John A</creatorcontrib><creatorcontrib>Margison, Geoffrey P</creatorcontrib><creatorcontrib>Williams, David M</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>AGRICOLA</collection><collection>AGRICOLA - 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>Wilkinson, Oliver J</au><au>Latypov, Vitaly</au><au>Tubbs, Julie L</au><au>Millington, Christopher L</au><au>Morita, Rihito</au><au>Blackburn, Hannah</au><au>Marriott, Andrew</au><au>McGown, Gail</au><au>Thorncroft, Mary</au><au>Watson, Amanda J</au><au>Connolly, Bernard A</au><au>Grasby, Jane A</au><au>Masui, Ryoji</au><au>Hunter, Christopher A</au><au>Tainer, John A</au><au>Margison, Geoffrey P</au><au>Williams, David M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation–π interactions</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-11-13</date><risdate>2012</risdate><volume>109</volume><issue>46</issue><spage>18755</spage><epage>18760</epage><pages>18755-18760</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O ⁶-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O ⁶-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O ⁶-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O ⁶-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O ⁶-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O ⁶-alkylguanines critical for NER recognition.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>23112169</pmid><doi>10.1073/pnas.1209451109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (46), p.18755-18760 |
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| subjects | adverse effects Alkyl and Aryl Transferases - chemistry Alkyl and Aryl Transferases - genetics Alkyl and Aryl Transferases - metabolism Alkylation Amino Acid Substitution Atomic interactions Atoms Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Biological Sciences Crystal structure Crystallography, X-Ray DNA DNA damage DNA repair DNA Repair - physiology guanine Guanine - chemistry Guanine - metabolism Hydrogen Lesions mechanics Molecular interactions mutants Mutation, Missense oligodeoxyribonucleotides Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - genetics Oligodeoxyribonucleotides - metabolism Physical Sciences Protein Binding Protein Structure, Tertiary proteins Purines Schizosaccharomyces - enzymology Schizosaccharomyces - genetics Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins - chemistry Schizosaccharomyces pombe Proteins - genetics Schizosaccharomyces pombe Proteins - metabolism Thermus thermophilus Thermus thermophilus - enzymology toxicity |
| title | Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation–π interactions |
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