Accepted name: GDP polyribonucleotidyltransferase
Reaction: (5′)pppAACA-[mRNA] + GDP = diphosphate + G(5′)pppAACA-[mRNA] (overall reaction)
(1a) (5′)pppAACA-[mRNA] + [protein L]-L-histidine = diphosphate + [protein L]-L-histidyl-(5′)phosphonato-AACA-[mRNA] + H2O
(1b) [protein L]-L-histidyl-(5′)phosphonato-AACA-[mRNA] + GDP + H2O = [protein L]-L-histidine + G(5′)pppAACA-[mRNA]
Other name(s): PRNTase; 5′-triphospho-mRNA:GDP 5′-phosphopolyribonucleotidyltransferase [G(5′)ppp-mRNA-forming]
Systematic name: (5′)pppAACA-[mRNA]:GDP 5′-phosphopolyribonucleotidyltransferase [(5′)pppAACA-[mRNA]-forming]
Comments: The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA. cf. EC, mRNA guanylyltransferase.
1.  Ogino, T. and Banerjee, A.K. Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol. Cell 25 (2007) 85–97. [PMID: 17218273]
2.  Ogino, T. and Banerjee, A.K. Formation of guanosine(5′)tetraphospho(5′)adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus. J. Virol. 82 (2008) 7729–7734. [PMID: 18495767]
3.  Ogino, T., Yadav, S.P. and Banerjee, A.K. Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase. Proc. Natl. Acad. Sci. USA 107 (2010) 3463–3468. [PMID: 20142503]
4.  Ogino, T. and Banerjee, A.K. The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity. J. Gen. Virol. 91 (2010) 1311–1314. [PMID: 20107017]
5.  Ogino, T. and Banerjee, A.K. An unconventional pathway of mRNA cap formation by vesiculoviruses. Virus Res. 162 (2011) 100–109. [PMID: 21945214]
6.  Ogino, M., Ito, N., Sugiyama, M. and Ogino, T. The rabies virus L protein catalyzes mRNA capping with GDP polyribonucleotidyltransferase activity. Viruses 8:144 (2016). [PMID: 27213429]
[EC created 2015, modified 2020]