Research output: Contribution to journal › Review article › peer-review
Transient protein–protein complexes in base excision repair. / Endutkin, Anton V.; Yudkina, Anna V.; Sidorenko, Viktoriya S. et al.
In: Journal of Biomolecular Structure and Dynamics, Vol. 37, No. 17, 22.11.2019, p. 4407-4418.Research output: Contribution to journal › Review article › peer-review
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TY - JOUR
T1 - Transient protein–protein complexes in base excision repair
AU - Endutkin, Anton V.
AU - Yudkina, Anna V.
AU - Sidorenko, Viktoriya S.
AU - Zharkov, Dmitry O.
PY - 2019/11/22
Y1 - 2019/11/22
N2 - Transient protein–protein complexes are of great importance for organizing multiple enzymatic reactions into productive reaction pathways. Base excision repair (BER), a process of critical importance for maintaining genome stability against a plethora of DNA-damaging factors, involves several enzymes, including DNA glycosylases, AP endonucleases, DNA polymerases, DNA ligases and accessory proteins acting sequentially on the same damaged site in DNA. Rather than being assembled into one stable multisubunit complex, these enzymes pass the repair intermediates between them in a highly coordinated manner. In this review, we discuss the nature and the role of transient complexes arising during BER as deduced from structural and kinetic data. Almost all of the transient complexes are DNA-mediated, although some may also exist in solution and strengthen under specific conditions. The best-studied example, the interactions between DNA glycosylases and AP endonucleases, is discussed in more detail to provide a framework for distinguishing between stable and transient complexes based on the kinetic data.
AB - Transient protein–protein complexes are of great importance for organizing multiple enzymatic reactions into productive reaction pathways. Base excision repair (BER), a process of critical importance for maintaining genome stability against a plethora of DNA-damaging factors, involves several enzymes, including DNA glycosylases, AP endonucleases, DNA polymerases, DNA ligases and accessory proteins acting sequentially on the same damaged site in DNA. Rather than being assembled into one stable multisubunit complex, these enzymes pass the repair intermediates between them in a highly coordinated manner. In this review, we discuss the nature and the role of transient complexes arising during BER as deduced from structural and kinetic data. Almost all of the transient complexes are DNA-mediated, although some may also exist in solution and strengthen under specific conditions. The best-studied example, the interactions between DNA glycosylases and AP endonucleases, is discussed in more detail to provide a framework for distinguishing between stable and transient complexes based on the kinetic data.
KW - AP endonucleases
KW - Base excision repair
KW - DNA glycosylases
KW - transient protein–protein complexes
UR - http://www.scopus.com/inward/record.url?scp=85059349538&partnerID=8YFLogxK
U2 - 10.1080/07391102.2018.1553741
DO - 10.1080/07391102.2018.1553741
M3 - Review article
C2 - 30488779
AN - SCOPUS:85059349538
VL - 37
SP - 4407
EP - 4418
JO - Journal of Biomolecular Structure and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
SN - 0739-1102
IS - 17
ER -
ID: 18066182