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J. Biol. Chem., Vol. 279, Issue 22, 23606-23614, May 28, 2004

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Phosphoprotein of the Rinderpest Virus Forms a Tetramer through a Coiled Coil Region Important for Biological Function

A STRUCTURAL INSIGHT^*

Abdur Rahaman, Naryanaswamy Srinivasan¶||, Narayanaswamy Shamala**, and Melkote Subbarao Shaila

From the Department of Microbiology and Cell Biology, the ^¶Molecular Biophysics Unit, and the ^**Department of Physics, Indian Institute of Science, Bangalore 560012, India

Phosphoprotein (P) of negative sense RNA viruses functions as a transcriptional transactivator of the viral polymerase (L). We report here the characterization of oligomeric P protein of rinderpest virus (RPV) and provide a structural basis for its multimerization. By size exclusion chromatography and dynamic light scattering analyses we show that bacterially expressed P protein exists as an oligomer, thus excluding the role of phosphorylation in P protein oligomerization. Gel filtration analyses of various parts of the P protein, also expressed in Escherichia coli, revealed that the predicted coiled coil region in the C-terminal domain is responsible for P protein oligomerization. Dynamic light scattering analysis confirmed the oligomeric nature of the coiled coil region of P. Chemical cross-linking analysis suggested that the C-terminal coiled coil region exists as a tetramer. The tetramer is formed by coiled coil interaction as shown by circular dichroism spectral analysis. Based on sequence homology, we propose a three-dimensional structure of the multimerization domain of RPV P using the crystal structure for multimerization domain of sendai virus (SeV) P as a template. Four-stranded coiled coil structure of the model is stabilized by a series of interactions predominantly between short nonpolar side chains emerging from different strands. In an in vivo replication/transcription system using a synthetic minigenome of RPV, we show that multimerization is essential for P protein function(s), and the multimerization domain is highly conserved between two morbilliviruses namely RPV and peste de petits ruminants virus. These results are discussed in the context of biological functions of P protein among various negative-stranded RNA viruses.

Received for publication, January 21, 2004 , and in revised form, March 16, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

A senior research fellow of the University Grant Commission, Government of India.

^|| Supported by the Senior Research Fellowship program for Biomedical Research by the Wellcome Trust, London.

To whom correspondence should be addressed: Dept. of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India. Tel.: 91-80-23600139/22932702; Fax: 91-80-23602697; E-mail: shaila{at}mcbl.iisc.ernet.in.

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