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J Virol, May 1998, p. 4274-4280, Vol. 72, No. 5
Department of Genetics and Microbiology,
University of Geneva Medical School, CH1211 Geneva, Switzerland
Received 16 September 1997/Accepted 10 February 1998
The SeV P protein is found as a homotrimer (P3) when it
is expressed in mammalian cells, and trimerization is mediated by a
predicted coiled-coil motif which maps within amino acids (aa) 344 to
411 (the BoxA region). The bacterially expressed protein also appears
to be trimeric, apparently precluding a role for phosphorylation in the
association of the P monomers. I have examined the role of P
trimerization both in the protein's interaction with the nucleocapsid
(N:RNA) template and in the protein's function on the template during
RNA synthesis. As with the results of earlier experiments
(32), I found that both the BoxA and BoxC (aa 479 to 568)
regions were required for stable binding of P to the N:RNA. Binding was
also observed with P proteins containing less than three BoxC regions,
suggesting that trimerization may be required to permit contacts
between multiple BoxC regions and the N:RNA. However, these
heterologous trimers failed to function in viral RNA synthesis,
indicating that the third C-terminal leg of the trimer plays an
essential role in P function on the template. We speculate that this
function may involve the movement of P (and possibly the polymerase
complex) on the template and the maintenance of processivity.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
A Role for the Sendai Virus P Protein Trimer in RNA
Synthesis
*
Mailing address: Department of Genetics and
Microbiology, University of Geneva Medical School, 9 avenue de Champel,
CH1211 Geneva, Switzerland. Phone: (41 22) 702 5727. Fax: (41 22) 702 5702. E-mail: curran{at}cmu.unige.ch.
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