Biology:APOBEC3C

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Short description: Protein-coding gene in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

DNA dC->dU-editing enzyme APOBEC-3C is a protein that in humans is encoded by the APOBEC3C gene.[1][2]

A3C belong to the A3 family of cytidine deaminases that act as restriction factors against diverse retroviruses. A3C was reported to inhibit simian immunodeficiency deficiency virus potently rather than HIV-1, in absence of viral infectivity factor, Vif.[3] Enhancing A3C's catalytic activity had only a marginal effect on HIV-1 replication (in absence of Vif), the counteractive viral mechanism is unclear.[4] A3C was also shown to inhibit other viruses.[5][6][7][8][9]

Function

This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. Conversely, A3 proteins enzymatically convert cytidine to uridine present in the single stranded DNA.[10][11][12][13][14] Two residues in loop 1 of A3C were demonstrated to determine its antiviral activity against HIV-1.[15]

Structure

The crystal structure of A3C suggests a putative HIV-1 vif binding region.[16][17] A3C was found to inhibit LINE-1 elements by directly interacting with ORF1p proteins, in a deaminase-independent manner.[18]

References

  1. ↑ "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics 79 (3): 285–96. March 2002. doi:10.1006/geno.2002.6718. PMID 11863358. 
  2. ↑ "Entrez Gene: APOBEC3C apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27350. 
  3. ↑ "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". The Journal of Biological Chemistry 279 (51): 53379–86. December 2004. doi:10.1074/jbc.M408802200. PMID 15466872. 
  4. ↑ "Enhancing the Catalytic Deamination Activity of APOBEC3C Is Insufficient to Inhibit Vif-Deficient HIV-1". Journal of Molecular Biology 429 (8): 1171–1191. April 2017. doi:10.1016/j.jmb.2017.03.015. PMID 28315663. 
  5. ↑ "Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C". Hepatology 46 (3): 682–9. September 2007. doi:10.1002/hep.21733. PMID 17625792. 
  6. ↑ "Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo". Journal of Virology 85 (15): 7594–602. August 2011. doi:10.1128/JVI.00290-11. PMID 21632763. 
  7. ↑ "Hypermutation of hepatitis B virus genomes by APOBEC3G, APOBEC3C and APOBEC3H". The Journal of General Virology 89 (Pt 5): 1184–91. May 2008. doi:10.1099/vir.0.83507-0. PMID 18420796. 
  8. ↑ "Core-APOBEC3C chimerical protein inhibits hepatitis B virus replication". Journal of Biochemistry 150 (4): 371–4. October 2011. doi:10.1093/jb/mvr086. PMID 21746770. 
  9. ↑ "APOBEC3A and 3C decrease human papillomavirus 16 pseudovirion infectivity". Biochemical and Biophysical Research Communications 457 (3): 295–9. February 2015. doi:10.1016/j.bbrc.2014.12.103. PMID 25576866. https://kanazawa-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=37760&item_no=1&attribute_id=31&file_no=1. 
  10. ↑ "Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome". Nature Structural & Molecular Biology 11 (5): 435–42. May 2004. doi:10.1038/nsmb758. PMID 15098018. 
  11. ↑ "RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators". Molecular Cell 10 (5): 1247–53. November 2002. doi:10.1016/s1097-2765(02)00742-6. PMID 12453430. 
  12. ↑ "DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses". Nature Immunology 4 (7): 641–3. July 2003. doi:10.1038/ni0703-641. PMID 12830140. 
  13. ↑ "DNA deamination mediates innate immunity to retroviral infection". Cell 113 (6): 803–9. June 2003. doi:10.1016/s0092-8674(03)00423-9. PMID 12809610. 
  14. ↑ "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication". The Journal of Biological Chemistry 279 (51): 53379–86. December 2004. doi:10.1074/jbc.M408802200. PMID 15466872. 
  15. ↑ Ayyappan Jaguva Vasudevan, Ananda; Balakrishnan, Kannan; G. W. Gertzen, Christoph; Borvető, Fanni; Zhang, Zeli; Sangwiman, Anucha; Held, Ulrike; Küstermann, Caroline et al. (October 2020). "Loop 1 of APOBEC3C regulates its antiviral activity against HIV-1" (in en). Journal of Molecular Biology 432 (23): 6200–6227. doi:10.1016/j.jmb.2020.10.014. PMID 33068636. https://linkinghub.elsevier.com/retrieve/pii/S0022283620305891. 
  16. ↑ "The APOBEC3C crystal structure and the interface for HIV-1 Vif binding". Nature Structural & Molecular Biology 19 (10): 1005–10. October 2012. doi:10.1038/nsmb.2378. PMID 23001005. 
  17. ↑ "Vif Proteins from Diverse Human Immunodeficiency Virus/Simian Immunodeficiency Virus Lineages Have Distinct Binding Sites in A3C". Journal of Virology 90 (22): 10193–10208. November 2016. doi:10.1128/JVI.01497-16. PMID 27581978. 
  18. ↑ "Human LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activity". Nucleic Acids Research 42 (1): 396–416. January 2014. doi:10.1093/nar/gkt898. PMID 24101588. 

Further reading

External links



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