Home LiteratureArticle Details
PMID: 27692063 Published · epublish English Journal Article

ATPase activity of the DEAD-box protein Dhh1 controls processing body formation.

eLife ·Vol. 5 ·2016-00-03

Mugler CF, Hondele M, Heinrich S, Sachdev R, Vallotton P, Koek AY, Chan LY, Weis K

Abstract

Translational repression and mRNA degradation are critical mechanisms of posttranscriptional gene regulation that help cells respond to internal and external cues. In response to certain stress conditions, many mRNA decay factors are enriched in processing bodies (PBs), cellular structures involved in degradation and/or storage of mRNAs. Yet, how cells regulate assembly and disassembly of PBs remains poorly understood. Here, we show that in budding yeast, mutations in the DEAD-box ATPase Dhh1 that prevent ATP hydrolysis, or that affect the interaction between Dhh1 and Not1, the central scaffold of the CCR4-NOT complex and an activator of the Dhh1 ATPase, prevent PB disassembly in vivo. Intriguingly, this process can be recapitulated in vitro, since recombinant Dhh1 and RNA, in the presence of ATP, phase-separate into liquid droplets that rapidly dissolve upon addition of Not1. Our results identify the ATPase activity of Dhh1 as a critical regulator of PB formation.

Keywords
DEAD box ATPases RNA turnover S. cerevisiae biochemistry cell biology processing bodies
MeSH Terms
Adenosine Triphosphatases/genetics,metabolism Cell Cycle Proteins/metabolism DEAD-box RNA Helicases/genetics,metabolism Macromolecular Substances/metabolism Mutant Proteins/genetics,metabolism RNA, Messenger/metabolism Saccharomyces cerevisiae/cytology,genetics,metabolism Saccharomyces cerevisiae Proteins/genetics,metabolism Transcription Factors/metabolism
Chemicals
CDC39 protein, S cerevisiae Cell Cycle Proteins Macromolecular Substances Mutant Proteins RNA, Messenger Saccharomyces cerevisiae Proteins Transcription Factors Adenosine Triphosphatases DHH1 protein, S cerevisiae DEAD-box RNA Helicases
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Mugler Christopher Frederick ORCID
University of California, Berkeley, Berkeley, United States.
Hondele Maria
ETH Zurich, Zurich, Switzerland.
Heinrich Stephanie ORCID
ETH Zurich, Zurich, Switzerland.
Sachdev Ruchika
ETH Zurich, Zurich, Switzerland.
Vallotton Pascal
ETH Zurich, Zurich, Switzerland.
Koek Adriana Y
University of California, Berkeley, Berkeley, United States.
Chan Leon Y
University of California, Berkeley, Berkeley, United States.
Weis Karsten ORCID
ETH Zurich, Zurich, Switzerland.
Conflict of Interest

KW: Reviewing editor, eLife. The other authors declare that no competing interests exist.

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Article Info
Journal
eLife
Abbr.
Elife
ISSN
2050-084X
DOI
10.7554/eLife.18746
Published
2016-00-03
Epub
2016-00-03
Language
English
Region
England
NLM ID
101579614
PMCID
PMC5096884
Subset
IM
Grants
NIGMS NIH HHS · R01 GM058065 · United States
NIGMS NIH HHS · R01 GM101257 · United States
NCRR NIH HHS · S10 RR027696 · United States
External Links
PubMed source DOI: 10.7554/eLife.18746 PMC Full Text View journal details
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