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Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair. / Rechkunova, Nadejda I.; Lavrik, Olga I.

In: Photochemistry and Photobiology, Vol. 96, No. 2, 01.03.2020, p. 440-449.

Research output: Contribution to journal › Review article › peer-review

Harvard

Rechkunova, NI & Lavrik, OI 2020, 'Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair', Photochemistry and Photobiology, vol. 96, no. 2, pp. 440-449. https://doi.org/10.1111/php.13222

APA

Rechkunova, N. I., & Lavrik, O. I. (2020). Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair. Photochemistry and Photobiology, 96(2), 440-449. https://doi.org/10.1111/php.13222

Vancouver

Rechkunova NI, Lavrik OI. Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair. Photochemistry and Photobiology. 2020 Mar 1;96(2):440-449. Epub 2020 Feb 3. doi: 10.1111/php.13222

Author

Rechkunova, Nadejda I. ; Lavrik, Olga I. / Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair. In: Photochemistry and Photobiology. 2020 ; Vol. 96, No. 2. pp. 440-449.

BibTeX

@article{8335d96e6ec142f6a8b40763e1b000f5,
title = "Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair",
abstract = "Replication protein A (RPA), eukaryotic single-stranded DNA-binding protein, is a key player in multiple processes of DNA metabolism including DNA replication, recombination and DNA repair. Human RPA composed of subunits of 70-, 32- and 14-kDa binds ssDNA with high affinity and interacts specifically with multiple proteins. The RPA heterotrimer binds ssDNA in several modes, with occlusion lengths of 8–10, 13–22 and 30 nucleotides corresponding to global, transitional and elongated conformations of protein. Varying the structure of photoreactive DNA, the intermediates of different stages of DNA replication or DNA repair were designed and applied to identify positioning of the RPA subunits on the specific DNA structures. Using this approach, RPA interactions with various types of DNA structures attributed to replication and DNA repair intermediates were examined. This review is dedicated to blessed memory of Prof. Alain Favre who contributed to the development of photoreactive nucleotide derivatives and their application for the study of protein–nucleic acids interactions.",
keywords = "SINGLE-STRANDED-DNA, NUCLEOTIDE EXCISION-REPAIR, PHOTO-CROSS-LINKING, TRANSFER-RNA SYNTHETASE, DAMAGE-RECOGNITION, PHOTOAFFINITY MODIFICATION, ESCHERICHIA-COLI, BINDING POLARITY, LARGE SUBUNIT, FACTOR C",
author = "Rechkunova, {Nadejda I.} and Lavrik, {Olga I.}",
note = "{\textcopyright} 2020 American Society for Photobiology.",
year = "2020",
month = mar,
day = "1",
doi = "10.1111/php.13222",
language = "English",
volume = "96",
pages = "440--449",
journal = "Photochemistry and Photobiology",
issn = "0031-8655",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair

AU - Rechkunova, Nadejda I.

AU - Lavrik, Olga I.

N1 - © 2020 American Society for Photobiology.

PY - 2020/3/1

Y1 - 2020/3/1

N2 - Replication protein A (RPA), eukaryotic single-stranded DNA-binding protein, is a key player in multiple processes of DNA metabolism including DNA replication, recombination and DNA repair. Human RPA composed of subunits of 70-, 32- and 14-kDa binds ssDNA with high affinity and interacts specifically with multiple proteins. The RPA heterotrimer binds ssDNA in several modes, with occlusion lengths of 8–10, 13–22 and 30 nucleotides corresponding to global, transitional and elongated conformations of protein. Varying the structure of photoreactive DNA, the intermediates of different stages of DNA replication or DNA repair were designed and applied to identify positioning of the RPA subunits on the specific DNA structures. Using this approach, RPA interactions with various types of DNA structures attributed to replication and DNA repair intermediates were examined. This review is dedicated to blessed memory of Prof. Alain Favre who contributed to the development of photoreactive nucleotide derivatives and their application for the study of protein–nucleic acids interactions.

AB - Replication protein A (RPA), eukaryotic single-stranded DNA-binding protein, is a key player in multiple processes of DNA metabolism including DNA replication, recombination and DNA repair. Human RPA composed of subunits of 70-, 32- and 14-kDa binds ssDNA with high affinity and interacts specifically with multiple proteins. The RPA heterotrimer binds ssDNA in several modes, with occlusion lengths of 8–10, 13–22 and 30 nucleotides corresponding to global, transitional and elongated conformations of protein. Varying the structure of photoreactive DNA, the intermediates of different stages of DNA replication or DNA repair were designed and applied to identify positioning of the RPA subunits on the specific DNA structures. Using this approach, RPA interactions with various types of DNA structures attributed to replication and DNA repair intermediates were examined. This review is dedicated to blessed memory of Prof. Alain Favre who contributed to the development of photoreactive nucleotide derivatives and their application for the study of protein–nucleic acids interactions.

KW - SINGLE-STRANDED-DNA

KW - NUCLEOTIDE EXCISION-REPAIR

KW - PHOTO-CROSS-LINKING

KW - TRANSFER-RNA SYNTHETASE

KW - DAMAGE-RECOGNITION

KW - PHOTOAFFINITY MODIFICATION

KW - ESCHERICHIA-COLI

KW - BINDING POLARITY

KW - LARGE SUBUNIT

KW - FACTOR C

UR - http://www.scopus.com/inward/record.url?scp=85081220099&partnerID=8YFLogxK

U2 - 10.1111/php.13222

DO - 10.1111/php.13222

M3 - Review article

C2 - 32017119

AN - SCOPUS:85081220099

VL - 96

SP - 440

EP - 449

JO - Photochemistry and Photobiology

JF - Photochemistry and Photobiology

SN - 0031-8655

IS - 2

ER -

ID: 23759154