Assembly of a dsRNA synthesizing complex RNA-DEPENDENT RNA POLYMERASE 2 contacts the largest subunit of NUCLEAR RNA POLYMERASE IV

In plants, transcription of selfish genetic elements such as transposons and DNA viruses is suppressed by RNA-directed DNA methylation. This process is guided by 24-nt short-interfering RNAs (siRNAs) whose double-stranded precursors are synthesized by DNA-dependent NUCLEAR RNA POLYMERASE IV (Pol IV)...

Full description

Saved in:

Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 118; no. 13; pp. 1 - 12
Main Authors:	Mishra, Vibhor, Singh, Jasleen, Wang, Feng, Zhang, Yixiang, Fukudom, Akihito, Trinidad, Jonathan C., Takagi, Yuichiro, Pikaard, Craig S.
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences 30-03-2021
Subjects:	Arabidopsis Proteins - genetics Arabidopsis Proteins - isolation & purification Arabidopsis Proteins - metabolism Biological Sciences Catalytic Domain - genetics DNA-Directed RNA Polymerases - genetics DNA-Directed RNA Polymerases - isolation & purification DNA-Directed RNA Polymerases - metabolism Molecular Docking Simulation Mutagenesis, Site-Directed Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism RNA, Double-Stranded - biosynthesis RNA-Dependent RNA Polymerase - genetics RNA-Dependent RNA Polymerase - isolation & purification RNA-Dependent RNA Polymerase - metabolism Two-Hybrid System Techniques gene silencing Pol IV RNA interference RDR2 RNA-directed DNA methylation
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	In plants, transcription of selfish genetic elements such as transposons and DNA viruses is suppressed by RNA-directed DNA methylation. This process is guided by 24-nt short-interfering RNAs (siRNAs) whose double-stranded precursors are synthesized by DNA-dependent NUCLEAR RNA POLYMERASE IV (Pol IV) and RNA-DEPENDENT RNA POLYMERASE 2 (RDR2). Pol IV and RDR2 coimmunoprecipitate, and their activities are tightly coupled, yet the basis for their association is unknown. Here, we show that an interval near the RDR2 active site contacts the Pol IV catalytic subunit, NRPD1, the largest of Pol IV’s 12 subunits. Contacts between the catalytic regions of the two enzymes suggests that RDR2 is positioned to rapidly engage the free 3′ ends of Pol IV transcripts and convert these single-stranded transcripts into double-stranded RNAs (dsRNAs).
Bibliography:	Author contributions: V.M., F.W., and C.S.P. designed research; V.M., J.S., F.W., Y.Z., J.C.T., and Y.T. performed research; Y.Z., A.F., J.C.T., and Y.T. contributed new reagents/analytic tools; V.M., Y.Z., A.F., J.C.T., and C.S.P. analyzed data; and V.M. and C.S.P. wrote the paper. Contributed by Craig S. Pikaard, February 17, 2021 (sent for review September 12, 2020; reviewed by Julie A. Law and R. Keith Slotkin) Reviewers: J.A.L., Salk Institute for Biological Studies; and R.K.S., Donald Danforth Plant Science Center.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.2019276118