Research output: Contribution to journal › Review article › peer-review
Noncatalytic Domains in DNA Glycosylases. / Torgasheva, Natalia A.; Diatlova, Evgeniia A.; Grin, Inga R. et al.
In: International Journal of Molecular Sciences, Vol. 23, No. 13, 7286, 01.07.2022.Research output: Contribution to journal › Review article › peer-review
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TY - JOUR
T1 - Noncatalytic Domains in DNA Glycosylases
AU - Torgasheva, Natalia A.
AU - Diatlova, Evgeniia A.
AU - Grin, Inga R.
AU - Endutkin, Anton V.
AU - Mechetin, Grigory V.
AU - Vokhtantsev, Ivan P.
AU - Yudkina, Anna V.
AU - Zharkov, Dmitry O.
N1 - Funding Information: Funding: The study was supported by the Russian Science Foundation (Grant No. 21-64-00017). I.R.G., A.V.E., I.P.V., and D.O.Z. acknowledge partial salary support from the Russian Ministry of Science and Education (Grant No. 121031300056-8). Publisher Copyright: © 2022 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2022/7/1
Y1 - 2022/7/1
N2 - Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.
AB - Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.
KW - base excision repair
KW - DNA binding
KW - DNA glycosylases
KW - DNA repair
KW - intrinsically disordered protein regions
KW - lesion search in DNA
KW - noncatalytic protein domains
KW - post-translational modifications
KW - protein–protein interactions
KW - Humans
KW - DNA/chemistry
KW - DNA Repair
KW - DNA Glycosylases/metabolism
KW - DNA Damage
UR - http://www.scopus.com/inward/record.url?scp=85133136227&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/e3ba57c3-68ec-3483-aa87-0b8886405abc/
U2 - 10.3390/ijms23137286
DO - 10.3390/ijms23137286
M3 - Review article
C2 - 35806289
AN - SCOPUS:85133136227
VL - 23
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1661-6596
IS - 13
M1 - 7286
ER -
ID: 36541420