Backbone and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes

被引：0

作者：

Gianluca A. Arianna

Dane H. Geddes-Buehre

Dmitry M. Korzhnev

机构：

[1] University of Connecticut Health Center,Department of Molecular Biology and Biophysics

来源：

Biomolecular NMR Assignments | 2023年 / 17卷

关键词：

Translesion synthesis; DNA damage tolerance; DNA repair; Protein-protein interactions; HORMA proteins;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Rev7 is a versatile HORMA (Hop1, Rev7, Mad2) family adaptor protein with multiple roles in mitotic regulation and DNA damage response, and an essential accessory subunit of the translesion synthesis (TLS) DNA polymerase Polζ employed in replication of damaged DNA. Within Polζ, the two copies of Rev7 interact with the two Rev7-bonding motifs (RBM1 and RBM2) of the catalytic subunit Rev3 by a mechanism characteristic of HORMA proteins whereby the “safety-belt” loop of Rev7 closes on the top of the ligand. Here we report the nearly complete backbone and Ile, Val, Leu side-chain methyl NMR resonance assignments of the 27 kDa human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes (BMRB deposition numbers 51651 and 51652) that will facilitate future NMR studies of Rev7 dynamics and interactions.

引用

页码：107 / 114

页数：7

共 25 条

[1] Backbone and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes
Arianna, Gianluca A.
Geddes-Buehre, Dane H.
Korzhnev, Dmitry M.
BIOMOLECULAR NMR ASSIGNMENTS, 2023, 17 (01) : 107 - 114
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[3] Crystal Structure of Human REV7 in Complex with a Human REV3 Fragment and Structural Implication of the Interaction between DNA Polymerase ζ and REV1
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JOURNAL OF BIOLOGICAL CHEMISTRY, 2010, 285 (16) : 12299 - 12307
[4] Purification, crystallization and initial X-ray diffraction study of human REV7 in complex with a REV3 fragment
Hara, Kodai
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Sato, Mamoru
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ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2009, 65 : 1302 - 1305
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Sobkowiak, Katarzyna
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Tropia, Laurence
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CELL REPORTS, 2025, 44 (04):
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Rajpal, DK
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MUTATION RESEARCH-DNA REPAIR, 2000, 461 (02): : 133 - 143
[7] REV7 is essential for DNA damage tolerance via two REV3L binding sites in mammalian DNA polymerase ζ
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NUCLEIC ACIDS RESEARCH, 2015, 43 (02) : 1000 - 1011
[8] The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζ
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[9] Overlapping in short motif sequences for binding to human REV7 and MAD2 proteins
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GENES TO CELLS, 2010, 15 (03) : 281 - 296
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Shimizu, Toshiyuki
Sato, Mamoru
Hashimoto, Hiroshi
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2012, 68 : 962 - 964

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