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Gene Review

APOBEC3F  -  apolipoprotein B mRNA editing enzyme,...

Homo sapiens

Synonyms: A3F, ARP8, BK150C2.4.MRNA, KA6
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Disease relevance of APOBEC3F

  • Indeed, the mutation spectra and expression profile found for APOBEC3F indicate that this enzyme, together with APOBEC3G, accounts for the G to A hypermutation of proviruses described in HIV-infected individuals [1].
  • Three of them, APOBEC3G, APOBEC3F, and APOBEC3B, block replication of human immunodeficiency virus type 1 (HIV-1) and many other retroviruses [2].
  • In opposition to APOBEC genes, HIV-1 and SIV contain a virion infectivity factor (Vif) that targets APOBEC3F and APOBEC3G for polyubiquitylation and proteasomal degradation [2].
  • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins [3].
  • G-->A hypermutation conforming to expected APOBEC3G polynucleotide sequence preferences was inferred in 9.4% (n = 12) of the HIV-1 sequences, with a further 2.4% (n = 3) conforming to APOBEC3F, and was independently associated with reduced pretreatment viremia (reduction of 0.7 log(10) copies/ml; P = 0.001) [4].

High impact information on APOBEC3F

  • Surprisingly, APOBEC3F and APOBEC3G are extensively coexpressed in nonpermissive human cells, including primary lymphocytes and the cell line CEM, where they form heterodimers [3].
  • Viral RNA and low-level DNA produced in the presence of APOBEC3F or rat APOBEC1 occasionally displayed mutations, but the majority of clones were wild-type [5].
  • Here, we have biochemically characterized human APOBEC3F and APOBEC3G protein complexes as a function of the HIV-1 life cycle [6].
  • The mechanism of L1 inhibition did not correlate with an obvious subcellular protein distribution as APOBEC3B appeared predominantly nuclear and APOBEC3F was mostly cytosolic [7].
  • A particularly high level of APOBEC3F protein in human testes and an inverse correlation between L1 activity and APOBEC3 gene number suggest the relevance of this mechanism to mammals [7].

Chemical compound and disease context of APOBEC3F


Biological context of APOBEC3F


Anatomical context of APOBEC3F


Associations of APOBEC3F with chemical compounds

  • Here, we show that only the C-terminal cytosine deaminase domain of APOBEC3F and -3G governs retroviral hypermutation [15].
  • We have exploited the fact that APOBEC3C, whilst highly homologous to the C-terminal domain of APOBEC3F, exhibits a distinct target site specificity (preferring Y-C dinucleotides) in order to identify residues in APOBEC3F that might affect its target site specificity [10].

Other interactions of APOBEC3F


  1. Cytidine deamination of retroviral DNA by diverse APOBEC proteins. Bishop, K.N., Holmes, R.K., Sheehy, A.M., Davidson, N.O., Cho, S.J., Malim, M.H. Curr. Biol. (2004) [Pubmed]
  2. Identification of APOBEC3DE as Another Antiretroviral Factor from the Human APOBEC Family. Dang, Y., Wang, X., Esselman, W.J., Zheng, Y.H. J. Virol. (2006) [Pubmed]
  3. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. Wiegand, H.L., Doehle, B.P., Bogerd, H.P., Cullen, B.R. EMBO J. (2004) [Pubmed]
  4. Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation. Pace, C., Keller, J., Nolan, D., James, I., Gaudieri, S., Moore, C., Mallal, S. J. Virol. (2006) [Pubmed]
  5. APOBEC-mediated interference with hepadnavirus production. Rösler, C., Köck, J., Kann, M., Malim, M.H., Blum, H.E., Baumert, T.F., von Weizsäcker, F. Hepatology (2005) [Pubmed]
  6. Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. Wang, X., Dolan, P.T., Dang, Y., Zheng, Y.H. J. Biol. Chem. (2007) [Pubmed]
  7. APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. Stenglein, M.D., Harris, R.S. J. Biol. Chem. (2006) [Pubmed]
  8. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. Tian, C., Yu, X., Zhang, W., Wang, T., Xu, R., Yu, X.F. J. Virol. (2006) [Pubmed]
  9. The Anti-HIV-1 Editing Enzyme APOBEC3G Binds HIV-1 RNA and Messenger RNAs That Shuttle between Polysomes and Stress Granules. Kozak, S.L., Marin, M., Rose, K.M., Bystrom, C., Kabat, D. J. Biol. Chem. (2006) [Pubmed]
  10. Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities. Langlois, M.A., Beale, R.C., Conticello, S.G., Neuberger, M.S. Nucleic Acids Res. (2005) [Pubmed]
  11. APOBEC deaminases as cellular antiviral factors: a novel natural host defense mechanism. Franca, R., Spadari, S., Maga, G. Med. Sci. Monit. (2006) [Pubmed]
  12. APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast. Schumacher, A.J., Nissley, D.V., Harris, R.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  13. Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins. J??nsson, S.R., Hach??, G., Stenglein, M.D., Fahrenkrug, S.C., Andr??sd??ttir, V., Harris, R.S. Nucleic Acids Res. (2006) [Pubmed]
  14. APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count. Cho, S.J., Drechsler, H., Burke, R.C., Arens, M.Q., Powderly, W., Davidson, N.O. J. Virol. (2006) [Pubmed]
  15. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. Haché, G., Liddament, M.T., Harris, R.S. J. Biol. Chem. (2005) [Pubmed]
  16. Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases. Dutko, J.A., Schäfer, A., Kenny, A.E., Cullen, B.R., Curcio, M.J. Curr. Biol. (2005) [Pubmed]
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