Picornaviral polymerase structure, function, and fidelity modulation.
Like all positive strand RNA viruses, the picornaviruses replicate their genomes using a virally encoded RNA-dependent RNA polymerase enzyme known as 3Dpol. Over the past decade we have made tremendous advances in our understanding of 3Dpolstructure and function, including the discovery of a novel mechanism for closing the active site that allows these viruses to easily fine tune replication fidelity and quasispecies distributions. This review summarizes current knowledge of picornaviral polymerase structure and how the enzyme interacts with RNA and other viral proteins to form stable and processive elongation complexes. The picornaviral RdRPs are among the smallest viral polymerases, but their fundamental molecular mechanism for catalysis appears to be generally applicable as a common feature of all positive strand RNA virus polymerases.
Department of Biochemistry & Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, United States. Electronic address: Olve.Peersen@ColoState.edu.
Olve B
OB
Peersen
D020134:Catalytic Domain; D010849:Picornaviridae / Q000201:enzymology* / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D012367:RNA, Viral / Q000378:metabolism; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry* / Q000378:metabolism*; D014158:Transcription, Genetic; D014764:Viral Proteins / Q000378:metabolism; D014779:Virus Replication
D012367:RNA, Viral; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase
Picornavirus; Polymerase; Positive strand RNA virus; RNA-dependent RNA polymerase; Structure