Nucleic Acids Research Advance Access originally published online on May 21, 2007
Nucleic Acids Research 2007 35(11):3774-3783; doi:10.1093/nar/gkm336
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Nucleic Acids Research, 2007, Vol. 35, No. 11 3774-3783
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
1Centro Nacional de Biotecnología (CSIC). Darwin 3, Campus de Cantoblanco. 28049 Madrid, Spain, 2Laboratoire de Virologie Moléculaire et Structurale, FRE 2854 CNRS-Université Joseph Fourier, Grenoble, France, 3EMBL Grenoble Outstation, c/o ILL, BP181, 38042 Grenoble Cedex 9, France and 4Centro de Investigaciones Biológicas (CSIC). Ramiro de Maeztu 9, Campus Universidad Complutense, 28040 Madrid, Spain
*To whom correspondence should be addressed. Tel: 34 91 837 3112 ext. 4446; Fax: 34 91 536 0432; Email: ollorca{at}cib.csic.es Correspondence may also be addressed to J. Ortín. Tel: 34 91 585 4557; Fax: 34-91 585 4506; Email: jortin{at}cnb.uam.es
Received March 16, 2007. Revised April 18, 2007. Accepted April 18, 2007.
The genome of influenza A virus is organized into eight ribonucleoprotein complexes (RNPs), each containing one RNA polymerase complex. This RNA polymerase has also been found non-associated to RNPs and is possibly involved in distinct functions in the infection cycle. We have expressed the virus RNA polymerase complex by co-tranfection of the PB1, PB2 and PA genes in mammalian cells and the heterotrimer was purified by the TAP tag procedure. Its 3D structure was determined by electron microscopy and single-particle image processing. The model obtained resembles the structure previously reported for the polymerase complex associated to viral RNPs but appears to be in a more open conformation. Detailed model comparison indicated that specific areas of the complex show important conformational changes as compared to the structure for the RNP-associated polymerase, particularly in regions known to interact with the adjacent NP monomers in the RNP. Also, the PB2 subunit seems to undergo a substantial displacement as a result of the association of the polymerase to RNPs. The structural model presented suggests that a core conformation of the polymerase in solution exists but the interaction with other partners, such as proteins or RNA, will trigger distinct conformational changes to activate new functional properties.
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