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Review
. 2015 May:29:166-79.
doi: 10.1016/j.dnarep.2015.02.011. Epub 2015 Feb 18.

Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins

Justyna McIntyre  1 , Roger Woodgate  2
Affiliations
Review

Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins

Justyna McIntyre et al. DNA Repair (Amst). 2015 May.

Abstract

Posttranslational modification of proteins often controls various aspects of their cellular function. Indeed, over the past decade or so, it has been discovered that posttranslational modification of lysine residues plays a major role in regulating translesion DNA synthesis (TLS) and perhaps the most appreciated lysine modification is that of ubiquitination. Much of the recent interest in ubiquitination stems from the fact that proliferating cell nuclear antigen (PCNA) was previously shown to be specifically ubiquitinated at K164 and that such ubiquitination plays a key role in regulating TLS. In addition, TLS polymerases themselves are now known to be ubiquitinated. In the case of human polymerase η, ubiquitination at four lysine residues in its C-terminus appears to regulate its ability to interact with PCNA and modulate TLS. Within the past few years, advances in global proteomic research have revealed that many proteins involved in TLS are, in fact, subject to a previously underappreciated number of lysine modifications. In this review, we will summarize the known lysine modifications of several key proteins involved in TLS; PCNA and Y-family polymerases η, ι, κ and Rev1 and we will discuss the potential regulatory effects of such modification in controlling TLS in vivo.

Keywords: PCNA; Translesion synthesis; Ubiquitin; Y-family polymerase.

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Conflict of interest statement

Conflict of interest

The authors declare no conflict of interest

Figures

Fig. 1
Fig. 1. Posttranslational modification of human PCNA
Lysines that have been indicated to be ubiquitinated are shown with a colored circle. Lysines that have been indicated to be acetylated are shown with a colored square. Lysines that have been indicated to be SUMOylated are shown by a colored triangle. The lysine residue that is ISGylated is shown by a red trapezium. The lysines that are known to be neddylated are shown by a green star. References are given in the appropriate associated box.
Fig. 2
Fig. 2. Posttranslational modification of human DNA polη
Lysines that have been identified to be ubiquitinated are shown with a colored circle. The serine residues that are thought to be phosphorylated, are shown by a colored star. References are given in the appropriate associated box.
Fig. 3
Fig. 3. Posttranslational modification of human DNA polι
Lysines that have been indicated to be ubiquitinated are shown with a colored circle and the appropriate reference cited in the associated box.
Fig. 4
Fig. 4. Posttranslational modification of human DNA polκ
Lysines that have been indicated to be ubiquitinated are shown with a colored circle. Lysines that have been indicated to be SUMOylated are shown by a colored triangle. The appropriate references are cited in the associated box.
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References

    1. Khoury GA, Baliban RC, Floudas CA. Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci. Rep. 2011;1 - PMC - PubMed
    1. Chen Y, Sprung R, Tang Y, Ball H, Sangras B, Kim SC, Falck JR, Peng J, Gu W, Zhao Y. Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol. Cell. Proteomics MCP. 2007;6:812–819. - PMC - PubMed
    1. Zhang X, Wen H, Shi X. Lysine methylation: beyond histones. Acta Biochim. Biophys. Sin. 2012;44:14–27. - PubMed
    1. Lee S. Post-translational modification of proteins in toxicological research: focus on lysine acylation. Toxicol. Res. 2013;29:81–86. - PMC - PubMed
    1. Friedberg EC, Friedberg EC. Eds DNA repair and mutagenesis. 2nd ed. Washington, D.C: ASM Press; 2006.

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