Open Access3D structure of the influenza virus polymerase complex: Localization of subunit domains
Author(s) -
Estela Área-Gómez,
Jaime MartínBenito,
Pablo Gastaminza,
Eva Torreira,
José Valpuesta,
José L. Carrascosa,
Juan Ortı́n
Publication year - 2003
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0307127101
Subject(s) - ribonucleoprotein , nucleoprotein , polymerase , rna polymerase , biology , microbiology and biotechnology , protein subunit , rna polymerase i , virology , rna dependent rna polymerase , virus , influenza a virus , rna , biochemistry , gene
The 3D structure of the influenza virus polymerase complex was determined by electron microscopy and image processing of recombinant ribonucleoproteins (RNPs). The RNPs were generated by in vivo amplification using cDNAs of the three polymerase subunits, the nucleoprotein, and a model virus-associated RNA containing 248 nt. The polymerase structure obtained is very compact, with no apparent boundaries among subunits. The position of specific regions of the PB1, PB2, and PA subunits was determined by 3D reconstruction of either RNP-mAb complexes or tagged RNPs. This structural model is available for the polymerase of a negative-stranded RNA virus and provides a general delineation of the complex and its interaction with the template-associated nucleoprotein monomers in the RNP.
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