1vpt

Structural highlights

Function

[MCE_VACCW] Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.^{[1] [2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Poly(A) Polymerase

References

1. ↑ Schnierle BS, Gershon PD, Moss B. Cap-specific mRNA (nucleoside-O2'-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2897-901. PMID:1313572
2. ↑ Gershon PD, Ahn BY, Garfield M, Moss B. Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus. Cell. 1991 Sep 20;66(6):1269-78. PMID:1670500
3. ↑ Latner DR, Thompson JM, Gershon PD, Storrs C, Condit RC. The positive transcription elongation factor activity of the vaccinia virus J3 protein is independent from its (nucleoside-2'-O-) methyltransferase and poly(A) polymerase stimulatory functions. Virology. 2002 Sep 15;301(1):64-80. PMID:12359447
4. ↑ Hodel AE, Gershon PD, Shi X, Quiocho FA. The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. Cell. 1996 Apr 19;85(2):247-56. PMID:8612277