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Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair

The interaction of xeroderma pigmentosum group A protein (XPA) and replication protein A (RPA) with damaged DNA in nucleotide excision repair (NER) was studied using model dsDNA and bubble-DNA structure with 5-{3-[6-(carboxyamido-fluoresceinyl)amidocapromoyl]allyl}-dUMP lesions in one strand and con...

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Autores principales: Krasikova, Yuliya S., Rechkunova, Nadejda I., Maltseva, Ekaterina A., Petruseva, Irina O., Lavrik, Olga I.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001049/
https://www.ncbi.nlm.nih.gov/pubmed/20693538
http://dx.doi.org/10.1093/nar/gkq649
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author Krasikova, Yuliya S.
Rechkunova, Nadejda I.
Maltseva, Ekaterina A.
Petruseva, Irina O.
Lavrik, Olga I.
author_facet Krasikova, Yuliya S.
Rechkunova, Nadejda I.
Maltseva, Ekaterina A.
Petruseva, Irina O.
Lavrik, Olga I.
author_sort Krasikova, Yuliya S.
collection PubMed
description The interaction of xeroderma pigmentosum group A protein (XPA) and replication protein A (RPA) with damaged DNA in nucleotide excision repair (NER) was studied using model dsDNA and bubble-DNA structure with 5-{3-[6-(carboxyamido-fluoresceinyl)amidocapromoyl]allyl}-dUMP lesions in one strand and containing photoreactive 5-iodo-dUMP residues in defined positions. Interactions of XPA and RPA with damaged and undamaged DNA strands were investigated by DNA–protein photocrosslinking and gel shift analysis. XPA showed two maximums of crosslinking intensities located on the 5′-side from a lesion. RPA mainly localized on undamaged strand of damaged DNA duplex and damaged bubble-DNA structure. These results presented for the first time the direct evidence for the localization of XPA in the 5′-side of the lesion and suggested the key role of XPA orientation in conjunction with RPA binding to undamaged strand for the positioning of the NER preincision complex. The findings supported the mechanism of loading of the heterodimer consisting of excision repair cross-complementing group 1 and xeroderma pigmentosum group F proteins by XPA on the 5′-side from the lesion before damaged strand incision. Importantly, the proper orientation of XPA and RPA in the stage of preincision was achieved in the absence of TFIIH and XPG.
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spelling pubmed-30010492010-12-13 Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair Krasikova, Yuliya S. Rechkunova, Nadejda I. Maltseva, Ekaterina A. Petruseva, Irina O. Lavrik, Olga I. Nucleic Acids Res Genome Integrity, Repair and Replication The interaction of xeroderma pigmentosum group A protein (XPA) and replication protein A (RPA) with damaged DNA in nucleotide excision repair (NER) was studied using model dsDNA and bubble-DNA structure with 5-{3-[6-(carboxyamido-fluoresceinyl)amidocapromoyl]allyl}-dUMP lesions in one strand and containing photoreactive 5-iodo-dUMP residues in defined positions. Interactions of XPA and RPA with damaged and undamaged DNA strands were investigated by DNA–protein photocrosslinking and gel shift analysis. XPA showed two maximums of crosslinking intensities located on the 5′-side from a lesion. RPA mainly localized on undamaged strand of damaged DNA duplex and damaged bubble-DNA structure. These results presented for the first time the direct evidence for the localization of XPA in the 5′-side of the lesion and suggested the key role of XPA orientation in conjunction with RPA binding to undamaged strand for the positioning of the NER preincision complex. The findings supported the mechanism of loading of the heterodimer consisting of excision repair cross-complementing group 1 and xeroderma pigmentosum group F proteins by XPA on the 5′-side from the lesion before damaged strand incision. Importantly, the proper orientation of XPA and RPA in the stage of preincision was achieved in the absence of TFIIH and XPG. Oxford University Press 2010-12 2010-08-06 /pmc/articles/PMC3001049/ /pubmed/20693538 http://dx.doi.org/10.1093/nar/gkq649 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Genome Integrity, Repair and Replication
Krasikova, Yuliya S.
Rechkunova, Nadejda I.
Maltseva, Ekaterina A.
Petruseva, Irina O.
Lavrik, Olga I.
Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title_full Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title_fullStr Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title_full_unstemmed Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title_short Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair
title_sort localization of xeroderma pigmentosum group a protein and replication protein a on damaged dna in nucleotide excision repair
topic Genome Integrity, Repair and Replication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001049/
https://www.ncbi.nlm.nih.gov/pubmed/20693538
http://dx.doi.org/10.1093/nar/gkq649
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