POLI simultaneously binds REV1 and monoUb:K164-PCNA at damaged DNA

Stable Identifier
R-HSA-5656105
Type
Reaction [binding]
Species
Homo sapiens
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DNA polymerase iota (POLI) is recruited to DNA damage sites through its interaction with PCNA and REV1. POLI has a functional PIP box in the C-terminus and two ubiquitin binding motifs (UBMs). The PIP box and UBMs are responsible for POLI binding to monoubiquitinated PCNA (MonoUb:K164-PCNA) (Bienko et al. 2005, Haracska et al. 2005, Bomar et al. 2010). The interaction between POLI and the C-terminus of REV1 is evolutionarily conserved (Kosarek et al. 2003, Guo et al. 2003, Ohashi et al. 2004). Since REV1 and POLI likely cooperate in the bypass of bulky DNA lesions (Yang et al. 2003) and the DNA polymerase zeta complex (POLZ) is needed for extension of nucleotides incorporated by POLI (Johnson et al. 2000), it is plausible that POLI forms a quaternary complex with REV1 and POLZ, as shown for POLK and proposed for other Y family DNA polymerases (Xie et al. 2012).

Literature References
PubMed ID Title Journal Year
15189446 Interaction of hREV1 with three human Y-family DNA polymerases

Ohashi, E, Murakumo, Y, Kanjo, N, Akagi, J, Masutani, C, Hanaoka, F, Ohmori, H

Genes Cells 2004
10984059 Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

Johnson, RE, Washington, MT, Haracska, L, Prakash, S, Prakash, L

Nature 2000
14657033 Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis

Guo, C, Fischhaber, PL, Luk-Paszyc, MJ, Masuda, Y, Zhou, J, Kamiya, K, Kisker, C, Friedberg, EC

EMBO J. 2003
15657443 A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesis

Haracska, L, Acharya, N, Unk, I, Johnson, RE, Hurwitz, J, Prakash, L, Prakash, S

Mol. Cell. Biol. 2005
12584190 Mammalian translesion DNA synthesis across an acrolein-derived deoxyguanosine adduct. Participation of DNA polymerase eta in error-prone synthesis in human cells

Yang, IY, Miller, H, Wang, Z, Frank, EG, Ohmori, H, Hanaoka, F, Moriya, M

J. Biol. Chem. 2003
20159559 Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1

Bomar, MG, D'Souza, S, Bienko, M, Dikic, I, Walker, GC, Zhou, P

Mol. Cell 2010
18242152 Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts

Kosarek, JN, Woodruff, RV, Rivera-Begeman, A, Guo, C, D'Souza, S, Koonin, EV, Walker, GC, Friedberg, EC

DNA Repair (Amst.) 2008
16357261 Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis

Bienko, M, Green, CM, Crosetto, N, Rudolf, F, Zapart, G, Coull, B, Kannouche, P, Wider, G, Peter, M, Lehmann, AR, Hofmann, K, Dikic, I

Science 2005
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