@article{Ma:2016:10.1016/j.jmb.2016.02.005,
author = {Ma, WK and Paudel, BP and Xing, Z and Sabath, IG and Rueda, D and Tran, EJ},
doi = {10.1016/j.jmb.2016.02.005},
journal = {Journal of Molecular Biology},
pages = {1091--1106},
title = {Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the Dead-Box RNA Helicase Dbp2 at Actively Transcribed Chromatin},
url = {http://dx.doi.org/10.1016/j.jmb.2016.02.005},
volume = {428},
year = {2016}
}

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TY  - JOUR
AB  - RNA helicases play fundamental roles in modulating RNA structures and facilitating RNA–protein (RNP) complex assembly in vivo. Previously, our laboratory demonstrated that the DEAD-box RNA helicase Dbp2 in Saccharomyces cerevisiae is required to promote efficient assembly of the co-transcriptionally associated mRNA-binding proteins Yra1, Nab2, and Mex67 onto poly(A)+ RNA. We also found that Yra1 associates directly with Dbp2 and functions as an inhibitor of Dbp2-dependent duplex unwinding, suggestive of a cycle of unwinding and inhibition by Dbp2. To test this, we undertook a series of experiments to shed light on the order of events for Dbp2 in co-transcriptional mRNP assembly. We now show that Dbp2 is recruited to chromatin via RNA and forms a large, RNA-dependent complex with Yra1 and Mex67. Moreover, single-molecule fluorescence resonance energy transfer and bulk biochemical assays show that Yra1 inhibits unwinding in a concentration-dependent manner by preventing the association of Dbp2 with single-stranded RNA. This inhibition prevents over-accumulation of Dbp2 on mRNA and stabilization of a subset of RNA polymerase II transcripts. We propose a model whereby Yra1 terminates a cycle of mRNP assembly by Dbp2.
AU  - Ma,WK
AU  - Paudel,BP
AU  - Xing,Z
AU  - Sabath,IG
AU  - Rueda,D
AU  - Tran,EJ
DO  - 10.1016/j.jmb.2016.02.005
EP  - 1106
PY  - 2016///
SN  - 1089-8638
SP  - 1091
TI  - Recruitment, Duplex Unwinding and Protein-Mediated Inhibition of the Dead-Box RNA Helicase Dbp2 at Actively Transcribed Chromatin
T2  - Journal of Molecular Biology
UR  - http://dx.doi.org/10.1016/j.jmb.2016.02.005
UR  - http://hdl.handle.net/10044/1/37464
VL  - 428
ER  - 

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