Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Cell. 2011 Jun 10;145(6):890-901. doi: 10.1016/j.cell.2011.05.010.

The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex.

Author information

  • 1Center for RNA Molecular Biology & Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.

Abstract

Many steps in nuclear RNA processing, surveillance, and degradation require TRAMP, a complex containing the poly(A) polymerase Trf4p, the Zn-knuckle protein Air2p, and the RNA helicase Mtr4p. TRAMP polyadenylates RNAs designated for decay or trimming by the nuclear exosome. It has been unclear how polyadenylation by TRAMP differs from polyadenylation by conventional poly(A) polymerase, which produces poly(A) tails that stabilize RNAs. Using reconstituted S. cerevisiae TRAMP, we show that TRAMP inherently suppresses poly(A) addition after only 3-4 adenosines. This poly(A) tail length restriction is controlled by Mtr4p. The helicase detects the number of 3'-terminal adenosines and, over several adenylation steps, elicits precisely tuned adjustments of ATP affinities and rate constants for adenylation and TRAMP dissociation. Our data establish Mtr4p as a critical regulator of polyadenylation by TRAMP and reveal that an RNA helicase can control the activity of another enzyme in a highly complex fashion and in response to features in RNA.

Copyright © 2011 Elsevier Inc. All rights reserved.

PMID:
21663793
[PubMed - indexed for MEDLINE]
PMCID:
PMC3115544
Free PMC Article

Images from this publication.See all images (8)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk