F
IPR004897

P/V phosphoprotein, paramyxoviral

InterPro entry
Short nameP/V_Pprotein_paramyxoviral

Description

Paramyxoviral P genes are able to generate more than one product, using alternative reading frames and RNA editing. The P gene encodes the structural phosphoprotein P. In addition, it encodes several non-structural proteins present in the infected cell but not in the virus particle. This family includes phosphoprotein P and the non-structural phosphoprotein V from different paramyxoviruses. Phosphoprotein P is a modular protein organised into two moieties that are both functionally and structurally distinct: a well-conserved C-terminal moiety that contains all the regions required for transcription, and a poorly conserved, intrinsically unstructured N-terminal moiety that provides several additional functions required for replication. The N-terminal moiety is responsible for binding to newly synthesized free N(0) (nucleoprotein that has not yet bound RNA), in order to prevent the binding of N(0) to cellular RNA. The C-terminal moiety consists of an oligomerisation domain, an N-RNA (nucleoprotein-RNA)-binding domain and an L polymerase-binding domain
[3, 4]
. Phosphoprotein P is essential for the activity of the RNA polymerase complex which it forms with the L subunit. Although all the catalytic activities of the polymerase are associated with the L subunit, its function requires specific interactions with phosphoprotein P
[1]
. The P and V phosphoproteins are amino co-terminal, but diverge at their C-termini. This difference is generated by an RNA-editing mechanism in which one or two non-templated G residues are inserted into P-gene-derived mRNA. In Measles virus and Sendai virus, one G residue is inserted and the edited transcript encodes the V protein. In Mumps virus, Simian virus 5 and Newcastle disease virus, two G residues are inserted, and the edited transcript codes for the P protein
[1]
. Being phosphoproteins, both P and V are rich in serine and threonine residues over their whole lengths. In addition, the V proteins are rich in cysteine residues at the C-termini
[2]
.

References

1.Two regions of the P protein are required to be active with the L protein for human parainfluenza virus type 1 RNA polymerase activity. Bousse T, Takimoto T, Matrosovich T, Portner A. Virology 283, 306-14, (2001). View articlePMID: 11336555

2.RNA editing in Newcastle disease virus. Steward M, Vipond IB, Millar NS, Emmerson PT. J. Gen. Virol. 74 ( Pt 12), 2539-47, (1993). PMID: 8277263

3.Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S. J. Biol. Chem. 278, 44567-73, (2003). View articlePMID: 12944395

4.Structural basis for the attachment of a paramyxoviral polymerase to its template. Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. Proc. Natl. Acad. Sci. U.S.A. 101, 8301-6, (2004). View articlePMID: 15159535

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