Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine
Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation...
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| Veröffentlicht in: | Biochemistry (Easton) 1986-11, Vol.25 (23), p.7362-7368 |
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| container_end_page | 7368 |
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| container_issue | 23 |
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| container_title | Biochemistry (Easton) |
| container_volume | 25 |
| creator | Brougham, Michael J Rowe, Thomas C Holloman, William K |
| description | Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation of the complex after removal of all but a small oligonucleotide fragment bound to the protein. The linkage of the Ustilago topoisomerase is to the 3' end of the broken strand of DNA. The DNA-protein complex formed is through a phosphodiester bond to tyrosine. |
| doi_str_mv | 10.1021/bi00371a018 |
| format | Article |
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Psychology ; Isomerases ; Kinetics ; phosphodiesters ; Protein Binding ; RECOMBINACION ; RECOMBINAISON ; RECOMBINATION ; Substrate Specificity ; TIROSINA ; TYROSINE ; USTILAGO ; Ustilago - enzymology</subject><ispartof>Biochemistry (Easton), 1986-11, Vol.25 (23), p.7362-7368</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a433t-9372ffac6bc7710b0c8a303e72d1d9acadbca206780eea64988c1361ce2ab7f43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00371a018$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00371a018$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8273407$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3026452$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brougham, Michael J</creatorcontrib><creatorcontrib>Rowe, Thomas C</creatorcontrib><creatorcontrib>Holloman, William K</creatorcontrib><title>Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation of the complex after removal of all but a small oligonucleotide fragment bound to the protein. The linkage of the Ustilago topoisomerase is to the 3' end of the broken strand of DNA. The DNA-protein complex formed is through a phosphodiester bond to tyrosine.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>ADN</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Basidiomycota - enzymology</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>DNA</subject><subject>DNA topoisomerase</subject><subject>DNA Topoisomerases, Type I - metabolism</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isomerases</subject><subject>Kinetics</subject><subject>phosphodiesters</subject><subject>Protein Binding</subject><subject>RECOMBINACION</subject><subject>RECOMBINAISON</subject><subject>RECOMBINATION</subject><subject>Substrate Specificity</subject><subject>TIROSINA</subject><subject>TYROSINE</subject><subject>USTILAGO</subject><subject>Ustilago - enzymology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc-L1DAUx4Mo67h68iYIOSx6kOpL0ibtcVl3VVz8wcwgeAmvaTqTtW3GpNWdi3-7kQ6DB8FDSB7fz_vy8r6EPGbwkgFnr2oHIBRDYOUdsmAFhyyvquIuWQCAzHgl4T55EONNKnNQ-Qk5EcBlXvAF-bXyO--i723AaGkbfE_XcXQdbjztcd-4SFsf-kiRGv8DOzuM6dHvOntLf7pxS6MbNp3N4hhwaGxDX384p-M2-GmzTT27rY_pNM7G0QZa-6Gho6fjPvjUaB-Sey120T463KdkfXW5unibXX988-7i_DrDXIgxq4TibYtG1kYpBjWYEgUIq3jDmgoNNrVBDlKVYC3KvCpLw4RkxnKsVZuLU_Js9t0F_31Ks-jeRWO7Dgfrp6iV4qIsefFfkOVFMucigS9m0KSfxGBbvQuux7DXDPSfWPRfsST66cF2qnvbHNlDDkk_O-gYDXZt2qVx8YiVXImUXMKyGXNpm7dHGcM3LZVQhV59WurPX9_DcqUq_SXxT2a-Ra9xE5LlelkqVlRSJvH5LKKJ-sZPYUgJ_HP638IbusI</recordid><startdate>19861118</startdate><enddate>19861118</enddate><creator>Brougham, Michael J</creator><creator>Rowe, Thomas C</creator><creator>Holloman, William K</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19861118</creationdate><title>Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine</title><author>Brougham, Michael J ; Rowe, Thomas C ; Holloman, William K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a433t-9372ffac6bc7710b0c8a303e72d1d9acadbca206780eea64988c1361ce2ab7f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>ADN</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Basidiomycota - enzymology</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>DNA</topic><topic>DNA topoisomerase</topic><topic>DNA Topoisomerases, Type I - metabolism</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Isomerases</topic><topic>Kinetics</topic><topic>phosphodiesters</topic><topic>Protein Binding</topic><topic>RECOMBINACION</topic><topic>RECOMBINAISON</topic><topic>RECOMBINATION</topic><topic>Substrate Specificity</topic><topic>TIROSINA</topic><topic>TYROSINE</topic><topic>USTILAGO</topic><topic>Ustilago - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brougham, Michael J</creatorcontrib><creatorcontrib>Rowe, Thomas C</creatorcontrib><creatorcontrib>Holloman, William K</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brougham, Michael J</au><au>Rowe, Thomas C</au><au>Holloman, William K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1986-11-18</date><risdate>1986</risdate><volume>25</volume><issue>23</issue><spage>7362</spage><epage>7368</epage><pages>7362-7368</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation of the complex after removal of all but a small oligonucleotide fragment bound to the protein. The linkage of the Ustilago topoisomerase is to the 3' end of the broken strand of DNA. The DNA-protein complex formed is through a phosphodiester bond to tyrosine.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>3026452</pmid><doi>10.1021/bi00371a018</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1986-11, Vol.25 (23), p.7362-7368 |
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| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADN Analytical, structural and metabolic biochemistry Basidiomycota - enzymology Binding Sites Biological and medical sciences DNA DNA topoisomerase DNA Topoisomerases, Type I - metabolism DNA, Single-Stranded - metabolism Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology Isomerases Kinetics phosphodiesters Protein Binding RECOMBINACION RECOMBINAISON RECOMBINATION Substrate Specificity TIROSINA TYROSINE USTILAGO Ustilago - enzymology |
| title | Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine |
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