Asset Details
Do you wish to reserve the book?
A mechanism for initiating RNA-dependent RNA polymerization
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
A mechanism for initiating RNA-dependent RNA polymerization
Do you wish to request the book?
A mechanism for initiating RNA-dependent RNA polymerization
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
A mechanism for initiating RNA-dependent RNA polymerization
2001
Overview
In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail
1
,
2
. Here we show that the 2 Å resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage φ6 (refs
3
,
4
) is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
Bacteriophage phi 6 - enzymology
/ Bacteriophage phi 6 - genetics
/ Biological and medical sciences
/ Fundamental and applied biological sciences. Psychology
/ Genomics
/ Humanities and Social Sciences
/ letter
/ Phage h6
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - metabolism
/ RNA
/ RNA, Double-Stranded - metabolism
/ RNA-Directed DNA Polymerase - chemistry
/ RNA-Directed DNA Polymerase - metabolism
/ Science
/ Structure in molecular biology
/ Viruses
