REV1 recruits POLZ to (AP:Cyt)-DNA Template

Stable Identifier
R-HSA-5652151
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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REV1, bound to the replication complex, recruits DNA polymerase zeta (POLZ, REV3L:MAD2L2) to the damaged DNA template. REV3L does not bind REV1 directly. Instead, REV3L binding to MAD2L2 (REV7) during the formation of POLZ complex causes a conformational change in MAD2L2 that allows the C-terminal domain of MAD2L2 to bind the C-terminus of REV1 (Nelson et al. 1996, Hara et al. 2010, Kikuchi et al. 2012, Xie et al. 2012)

Literature References
PubMed ID Title Journal Year
8751446 Deoxycytidyl transferase activity of yeast REV1 protein

Nelson, JR, Lawrence, CW, Hinkle, DC

Nature 1996
23143872 Structural insights into the assembly of human translesion polymerase complexes

Xie, W, Yang, X, Xu, M, Jiang, T

Protein Cell 2012
22859296 Structural basis of recruitment of DNA polymerase ? by interaction between REV1 and REV7 proteins

Kikuchi, S, Hara, K, Shimizu, T, Sato, M, Hashimoto, H

J. Biol. Chem. 2012
20164194 Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1

Hara, K, Hashimoto, H, Murakumo, Y, Kobayashi, S, Kogame, T, Unzai, S, Akashi, S, Takeda, S, Shimizu, T, Sato, M

J. Biol. Chem. 2010
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