Y-box binding protein 1 (YB-1) promotes detection of DNA bulky lesions by XPC-HR23B factor
The nucleotide excision repair system (NER) is one of the main mechanisms protecting cellular DNA from lesions caused by such significant environmental factors as UV radiation, the influence of polycyclic aromatic hydrocarbons, and medical treatment by several antitumor drugs, e.g. cisplatin. One of...
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| Veröffentlicht in: | Biochemistry (Moscow) 2015-02, Vol.80 (2), p.219-227 |
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| creator | Fomina, E. E. Pestryakov, P. E. Maltseva, E. A. Petruseva, I. O. Kretov, D. A. Ovchinnikov, L. P. Lavrik, O. I. |
| description | The nucleotide excision repair system (NER) is one of the main mechanisms protecting cellular DNA from lesions caused by such significant environmental factors as UV radiation, the influence of polycyclic aromatic hydrocarbons, and medical treatment by several antitumor drugs, e.g. cisplatin. One of the major NER components is XPC-HR23B, the key factor during the damage recognition step of repair. Binding of XPC-HR23B to DNA that contains different bulky lesions impairing the structure of DNA is the basis for the wide substrate specificity of this DNA repair pathway. The multifunctional protein YB-1 among other protein factors has high affinity towards damaged DNA. Involvement of YB-1 in the cellular response to genotoxic stress and its ability to interact with damaged DNA harboring lesions of various origins pinpoint its putative involvement as a modulatory factor in DNA damage recognition and verification steps of NER. In the present work, we assayed functional interactions of protein factors XPC-HR23B and YB-1 upon binding to DNA structures mimicking damaged DNA containing single bulky lesions, as substrates of NER, and bulky lesions combined with abasic sites as an example of clustered lesions. The results indicate that YB-1 and XPC-HR23B stimulate each other in binding to DNA containing a bulky or clustered lesion, which suggests the involvement of YB-1 in the regulation of DNA repair by the NER mechanism. |
| doi_str_mv | 10.1134/S000629791502008X |
| format | Article |
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E. ; Pestryakov, P. E. ; Maltseva, E. A. ; Petruseva, I. O. ; Kretov, D. A. ; Ovchinnikov, L. P. ; Lavrik, O. I.</creator><creatorcontrib>Fomina, E. E. ; Pestryakov, P. E. ; Maltseva, E. A. ; Petruseva, I. O. ; Kretov, D. A. ; Ovchinnikov, L. P. ; Lavrik, O. I.</creatorcontrib><description>The nucleotide excision repair system (NER) is one of the main mechanisms protecting cellular DNA from lesions caused by such significant environmental factors as UV radiation, the influence of polycyclic aromatic hydrocarbons, and medical treatment by several antitumor drugs, e.g. cisplatin. One of the major NER components is XPC-HR23B, the key factor during the damage recognition step of repair. Binding of XPC-HR23B to DNA that contains different bulky lesions impairing the structure of DNA is the basis for the wide substrate specificity of this DNA repair pathway. The multifunctional protein YB-1 among other protein factors has high affinity towards damaged DNA. Involvement of YB-1 in the cellular response to genotoxic stress and its ability to interact with damaged DNA harboring lesions of various origins pinpoint its putative involvement as a modulatory factor in DNA damage recognition and verification steps of NER. In the present work, we assayed functional interactions of protein factors XPC-HR23B and YB-1 upon binding to DNA structures mimicking damaged DNA containing single bulky lesions, as substrates of NER, and bulky lesions combined with abasic sites as an example of clustered lesions. The results indicate that YB-1 and XPC-HR23B stimulate each other in binding to DNA containing a bulky or clustered lesion, which suggests the involvement of YB-1 in the regulation of DNA repair by the NER mechanism.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S000629791502008X</identifier><identifier>PMID: 25756536</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Binding sites ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Deoxyribonucleic acid ; DNA ; DNA - metabolism ; DNA Adducts - metabolism ; DNA binding proteins ; DNA Repair ; DNA Repair Enzymes - metabolism ; DNA-Binding Proteins - metabolism ; Environmental factors ; Health aspects ; Humans ; Lesions ; Life Sciences ; Medical treatment ; Microbiology ; Polycyclic aromatic hydrocarbons ; Protein research ; Proteins ; Substrate Specificity ; Ultraviolet radiation ; Y-Box-Binding Protein 1 - metabolism</subject><ispartof>Biochemistry (Moscow), 2015-02, Vol.80 (2), p.219-227</ispartof><rights>Pleiades Publishing, Ltd. 2015</rights><rights>COPYRIGHT 2015 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-9e07b0dbbb764eec5b9dfc2ca9e217323868d376100d1648d81517388f1de8d93</citedby><cites>FETCH-LOGICAL-c520t-9e07b0dbbb764eec5b9dfc2ca9e217323868d376100d1648d81517388f1de8d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S000629791502008X$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S000629791502008X$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25756536$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fomina, E. 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Binding of XPC-HR23B to DNA that contains different bulky lesions impairing the structure of DNA is the basis for the wide substrate specificity of this DNA repair pathway. The multifunctional protein YB-1 among other protein factors has high affinity towards damaged DNA. Involvement of YB-1 in the cellular response to genotoxic stress and its ability to interact with damaged DNA harboring lesions of various origins pinpoint its putative involvement as a modulatory factor in DNA damage recognition and verification steps of NER. In the present work, we assayed functional interactions of protein factors XPC-HR23B and YB-1 upon binding to DNA structures mimicking damaged DNA containing single bulky lesions, as substrates of NER, and bulky lesions combined with abasic sites as an example of clustered lesions. The results indicate that YB-1 and XPC-HR23B stimulate each other in binding to DNA containing a bulky or clustered lesion, which suggests the involvement of YB-1 in the regulation of DNA repair by the NER mechanism.</description><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA Adducts - metabolism</subject><subject>DNA binding proteins</subject><subject>DNA Repair</subject><subject>DNA Repair Enzymes - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Environmental factors</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Lesions</subject><subject>Life Sciences</subject><subject>Medical treatment</subject><subject>Microbiology</subject><subject>Polycyclic aromatic hydrocarbons</subject><subject>Protein research</subject><subject>Proteins</subject><subject>Substrate Specificity</subject><subject>Ultraviolet radiation</subject><subject>Y-Box-Binding Protein 1 - metabolism</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkUtv1TAQhS0EopfCD2CDLLEpi5SxHT-yvL08ilQB4iG1bKLYnly5JHEbJxL33-PoFlReEvJi5DPfOZrREPKYwTFjonz-EQAUr3TFJHAAc36HrJgCUwgo4S5ZLe1i6R-QByld5i-HStwnB1xqqaRQK_LlorDxG7Vh8GHY0qsxThgGyujRxUnBni1Cn6VEPU7ophAHGlv64u2a2rn7uqMdpqwlanf0_P2mOP3AxQltGzfF8SG51zZdwkc39ZB8fvXy0-a0OHv3-s1mfVY4yWEqKgRtwVtrtSoRnbSVbx13TYWcacGFUcYLrRiAZ6o03jCZdWNa5tH4ShySo31unvV6xjTVfUgOu64ZMM6pZkoZLqHS_H9QroThQmT06W_oZZzHIS-SKSlVHojforZNh3UY2jiNjVtC63UJWqmKgc7U8V-o_Dz2wcUB25D1Xwxsb3BjTGnEtr4aQ9-Mu5pBvZy-_uP02fPkZuDZ9uh_On7cOgN8D6TcGrY43tron6nfAXRosgw</recordid><startdate>20150201</startdate><enddate>20150201</enddate><creator>Fomina, E. 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E.</au><au>Pestryakov, P. E.</au><au>Maltseva, E. A.</au><au>Petruseva, I. O.</au><au>Kretov, D. A.</au><au>Ovchinnikov, L. P.</au><au>Lavrik, O. I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Y-box binding protein 1 (YB-1) promotes detection of DNA bulky lesions by XPC-HR23B factor</atitle><jtitle>Biochemistry (Moscow)</jtitle><stitle>Biochemistry Moscow</stitle><addtitle>Biochemistry (Mosc)</addtitle><date>2015-02-01</date><risdate>2015</risdate><volume>80</volume><issue>2</issue><spage>219</spage><epage>227</epage><pages>219-227</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><abstract>The nucleotide excision repair system (NER) is one of the main mechanisms protecting cellular DNA from lesions caused by such significant environmental factors as UV radiation, the influence of polycyclic aromatic hydrocarbons, and medical treatment by several antitumor drugs, e.g. cisplatin. One of the major NER components is XPC-HR23B, the key factor during the damage recognition step of repair. Binding of XPC-HR23B to DNA that contains different bulky lesions impairing the structure of DNA is the basis for the wide substrate specificity of this DNA repair pathway. The multifunctional protein YB-1 among other protein factors has high affinity towards damaged DNA. Involvement of YB-1 in the cellular response to genotoxic stress and its ability to interact with damaged DNA harboring lesions of various origins pinpoint its putative involvement as a modulatory factor in DNA damage recognition and verification steps of NER. In the present work, we assayed functional interactions of protein factors XPC-HR23B and YB-1 upon binding to DNA structures mimicking damaged DNA containing single bulky lesions, as substrates of NER, and bulky lesions combined with abasic sites as an example of clustered lesions. 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| subjects | Binding sites Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Deoxyribonucleic acid DNA DNA - metabolism DNA Adducts - metabolism DNA binding proteins DNA Repair DNA Repair Enzymes - metabolism DNA-Binding Proteins - metabolism Environmental factors Health aspects Humans Lesions Life Sciences Medical treatment Microbiology Polycyclic aromatic hydrocarbons Protein research Proteins Substrate Specificity Ultraviolet radiation Y-Box-Binding Protein 1 - metabolism |
| title | Y-box binding protein 1 (YB-1) promotes detection of DNA bulky lesions by XPC-HR23B factor |
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