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Review
. 2019 Jul 3;20(13):3279.
doi: 10.3390/ijms20133279.

Isoforms of Base Excision Repair Enzymes Produced by Alternative Splicing

Elizaveta O Boldinova  1 , Rafil F Khairullin  2 , Alena V Makarova  3 , Dmitry O Zharkov  4   5
Affiliations
Review

Isoforms of Base Excision Repair Enzymes Produced by Alternative Splicing

Elizaveta O Boldinova et al. Int J Mol Sci. .

Abstract

Transcripts of many enzymes involved in base excision repair (BER) undergo extensive alternative splicing, but functions of the corresponding alternative splice variants remain largely unexplored. In this review, we cover the studies describing the common alternatively spliced isoforms and disease-associated variants of DNA glycosylases, AP-endonuclease 1, and DNA polymerase beta. We also discuss the roles of alternative splicing in the regulation of their expression, catalytic activities, and intracellular transport.

Keywords: DNA glycosylases; DNA polymerase beta; alternative splicing; apurinic/apyrimidinic endonuclease.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Organization of the alternative transcription initiation in the human UNG gene. Untranslated regions are yellow, coding sequences are green. MTS—mitochondrial _targeting sequence.
Figure 2
Figure 2
(A) Organization of exons 4–8 and alternative splicing products of the human OGG1 gene. (B) Structure of OGG1-1a protein (PDB ID 1EBM, [98]). DNA backbone is shown schematically as an orange line. The protein part encoded by exon 7 and thus missing in OGG1-1b and all group 2 isoforms are colored red. Phe319 forms a wall of the enzyme active site and stacks against the oxoG base; these interactions have to be remodeled in OGG1 group 2. Untranslated regions are yellow, coding sequences are green.
Figure 3
Figure 3
The schematic intron–exon organization of the human POLB gene and its common alternative splicing products. Untranslated regions are yellow, coding sequences are green.
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