8wqq

Structural highlights

Function

DIPP_ASFB7 Decapping enzyme required for the removal of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow their decay in cells (PubMed:19695654). May therefore accelerate viral and cellular mRNA turnover to eliminate competing host mRNAs and allow stage-specific synthesis of viral proteins. Acceleration of the turnover of cellular transcripts may even promote the shutoff of host protein synthesis (PubMed:29021398). In addition to the mRNA cap, g5R also efficiently hydrolyzes diphosphoinositol polyphosphates. Down-regulation of the level of PP-InsP5 (diphosphoinositol pentakisphosphate) may play a role in viral manipulation of the cellular secretory pathway, a step necessary for the formation of virions (PubMed:11773415). Binds viral and cellular poly(A) mRNAs, thereby decreasing both types of mRNAs (PubMed:19695654, PubMed:29021398).^{[1] [2] [3]}

References

1. ↑ Cartwright JL, Safrany ST, Dixon LK, Darzynkiewicz E, Stepinski J, Burke R, McLennan AG. The g5R (D250) gene of African swine fever virus encodes a Nudix hydrolase that preferentially degrades diphosphoinositol polyphosphates. J Virol. 2002 Feb;76(3):1415-21. doi: 10.1128/jvi.76.3.1415-1421.2002. PMID:11773415 doi:http://dx.doi.org/10.1128/jvi.76.3.1415-1421.2002
2. ↑ Parrish S, Hurchalla M, Liu SW, Moss B. The African swine fever virus g5R protein possesses mRNA decapping activity. Virology. 2009 Oct 10;393(1):177-82. doi: 10.1016/j.virol.2009.07.026. Epub 2009 , Aug 19. PMID:19695654 doi:http://dx.doi.org/10.1016/j.virol.2009.07.026
3. ↑ Quintas A, Perez-Nunez D, Sanchez EG, Nogal ML, Hentze MW, Castello A, Revilla Y. Characterization of the African Swine Fever Virus Decapping Enzyme during Infection. J Virol. 2017 Nov 30;91(24):e00990-17. doi: 10.1128/JVI.00990-17. Print 2017 Dec , 15. PMID:29021398 doi:http://dx.doi.org/10.1128/JVI.00990-17