A PRESPECTIVE STUDY ON APOBEC PROTEIN FAMILY

  • S. GEJALAKSHMI Faculty of Pharmacy, Department of Pharmaceutical Chemistry Dr. M. G. R. Educational and Research Institute, Velappanchavadi, Chennai-77
  • N. HARIKRISHNAN Faculty of Pharmacy, Department of Pharmaceutical Chemistry Dr. M. G. R. Educational and Research Institute, Velappanchavadi, Chennai-77
  • S. KOMAL Faculty of Pharmacy, Department of Pharmaceutical Chemistry Dr. M. G. R. Educational and Research Institute, Velappanchavadi, Chennai-77

Abstract

Apobec is an apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like" is a family of deaminases. It has two types of APOBEC enzymes n-terminal of apobec enzyme and C-terminal of APOBEC enzyme. N-terminal domain is catalytic domain and C-terminal domain is a pseudo catalytic domain. Pathogen and cellular genome undergo mutation by human DNA cytosine to uracil deaminases. Three subtypes of APOBEC3D. APOBEC3F, APOBEC3G and APOBEC3H restrict human deficiency virus-1. Two APOBEC enzymes are the sources of somatic mutagenesis in cancer cells that drive tumor evolution and manifest clinically as theraphy resistance. This review of the APOBEC family will focus on an open question in regulation, namely what role the interactions of these proteins with RNA have in editing substrate recognition or allosteric regulation of DNA mutagenic and host-defense activities.

Keywords: APOBEC, DNA mutagen, m-RNA

References

1. Gerlinger M, McGranahan N, Dewhurst SM, Burrell RA, Tomlinson I, Swanton C. Cancer: evolution within a lifetime. Ann Rev Gen 2014;48:215–36.
2. Roberts SA, Gordenin DA. Hypermutation in human cancer genomes: footprints and mechanisms. Nat Rev Cancer 2014;14:786–800.
3. Burns MB, Leonard B, Harris RS. APOBEC3B: pathological consequences of an innate immune DNA mutator. Biomed J 2015;38:102–10.
4. Henderson S, Fenton T. APOBEC3 genes: retroviral restriction factors to cancer drivers. Trends Mol Med 2015;21:274–84.
5. Harris RS. Molecular mechanism and clinical impact of APOBEC3B-catalyzed mutagenesis in breast cancer. Breast Cancer Res 2015;17:8.
6. Harris RS, Petersen Mahrt SK, Neuberger MS. RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol Cell 2002;10:1247–53.
7. Petersen Mahrt SK, Harris RS, Neuberger MS. AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature 2002;418:99–103.
8. Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002;418:646–50.
9. Madison B Adolph, Robin P Love, Linda Chelico. Apobec enzymes as targets for virus and cancer therapy. Cell Chem Biol 2018;25:36–49.
10. Jeffrey Chen, Thomas MacCarthy. The preferred nucleotide contexts of the AID/APOBEC cytidine deaminases have differential effects when mutating retrotransposon and virus sequences compared to host genes. PLOS Comput Biol 2017;13:e1005471.
11. Shraddha Sharma, Santosh K Patnaik, Robert T Taggart, Bora E Baysal. The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme. Sci Rep 2016;6:39100.
12. Uqing Feng, Tayyba T Baig, Robin P Love, Linda Chelico, Yuqing Feng, Tayyba T Baig, et al. Suppression of APOBEC3-mediated restriction of HIV. Front Microbiol 2014;5:450.
13. Spyridon Stavrou, Susan R. Ross APOBEC3 proteins in viral immunity. J Immunol 2015;195:4565–70.
14. Kimberly M Prohaska, Ryan P Bennett, Jason D Salter, Harold C Smith. The multifaceted roles of RNAbinding in APOBEC cytidinedeaminase functions. Wiley Interdiscip Rev RNA 2014;5:493-508.
15. Naveenan Navaratnam. Rizwan sarwar an overview of cytidine deaminases. Int J Hematol 2006;83:195-200.
16. Jianlong Gao, Hani Choudhry, Wei Cao. Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like family genes activation and regulation during tumorigenesis. Cancer Sci 2018;109:2375–82.
17. Benjamin JM Taylor, Serena Nik-Zainal, Yee Ling Wu, Lucy A Stebbings, Keiran Raine, Peter J Campbell, Cristina Rada, et al. DNA deaminases induce break-associated mutation showers with implication of APOBEC3B and 3A in breast cancer kataegis. Elife 2013;2:e00534.
18. Sara L Sawyer, Michael Emerman, Harmit S Malik. Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G. PLoS Biol 2004;2:e275.
19. Stephen J Hollanda, Lesley M Berghuisb, Justin J Kingb, Lakshminarayan M Iyerc, Katarzyna Sikoraa. Expansions, diversification, and interindividual copy number variations of AID/APOBEC family cytidine deaminase genes in lampreys. PLoS Biol 2004;115:E3211-E3220.
20. Stephen J Hollanda, Lesley M Berghuisb, Justin J Kingb, Lakshminarayan M Iyerc, Katarzyna Sikoraa, Heather Fifieldb, et al. Expansions, diversification, and interindividual copy number variations of AID/APOBEC family cytidine deaminase genes in lampreys. PNAS 2018;115:E3211–E3220.
21. Shraddha Sharma, Jianmin Wang, Scott Portwood, Eduardo Cortes-Gomez, Orla Maguire. Mitochondrial hypoxic stress induces widespread RNA editing by 1 APOBEC3G in lymphocytes Genome Biol 2019;20:37.
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GEJALAKSHMI, S., N. HARIKRISHNAN, and S. KOMAL. “A PRESPECTIVE STUDY ON APOBEC PROTEIN FAMILY”. International Journal of Current Pharmaceutical Research, Vol. 11, no. 6, Nov. 2019, pp. 15-18, doi:10.22159/ijcpr.2019v11i6.36345.
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Review Article(s)