Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Analysis of recombinant yeast decapping enzyme.

Michelle Steiger1, Anne Carr-Schmid, David C Schwartz

  • 1Department of Molecular and Cellular Biology & Howard Hughes Medical Institute, University of Arizona, 1007 E. Lowell Street, Tucson, AZ 85704, USA.

RNA (New York, N.Y.)
|January 30, 2003
PubMed
Summary

Yeast mRNA decapping requires Dcp1p and Dcp2p proteins. Researchers found Dcp2p acts as a catalytic subunit, with Dcp1p enhancing its activity, and identified RNA-binding sites crucial for decapping.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Nuclear tau aggregates inhibit RNA export and form by secondary seeding from cytosolic tau aggregates.

bioRxiv : the preprint server for biology·2026
Same author

Base Composition Influences the Position and Precision of RNA Polymerase II Disassociation in Basal and Perturbed Conditions.

bioRxiv : the preprint server for biology·2026
Same author

Polyserine domains are toxic and exacerbate tau pathology in mice.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Nucleic acid-protein condensates in innate immunity.

Molecular cell·2025
Same author

DHX36 modulates stress granule assembly independent of recruitment of mRNAs with G-quadruplex sequence motifs.

Nucleic acids research·2025
Same author

Polyserine-mediated targeting of FAF2/UBXD8 ameliorates tau aggregation.

Neuron·2025

Area of Science:

  • Molecular Biology
  • Yeast Genetics
  • Enzymology

Background:

  • mRNA decapping is essential for yeast mRNA turnover.
  • The roles of Dcp1p and Dcp2p in decapping are not fully understood.

Purpose of the Study:

  • To elucidate the specific functions of Dcp1p and Dcp2p in the yeast decapping reaction.
  • To characterize the biochemical properties of recombinant Dcp1p and Dcp2p.

Main Methods:

  • Purification of recombinant Dcp1p and Dcp2p from E. coli.
  • In vitro biochemical assays to assess decapping activity.
  • Investigation of substrate preference and inhibition patterns.
  • Reconstitution of decapping activation using other proteins.

Main Results:

Related Experiment Videos

  • Copurified Dcp1p and Dcp2p form an active decapping enzyme.
  • Dcp2p exhibits catalytic activity independently under certain conditions.
  • The Dcp1p/Dcp2p complex prefers longer mRNA substrates and has a distinct RNA-binding site.
  • Edc1p and Edc2p directly activate the decapping enzyme.

Conclusions:

  • Dcp2p is likely the catalytic subunit of the decapping complex.
  • Dcp1p may enhance Dcp2p activity or act as an additional subunit.
  • The decapping enzyme possesses an RNA-binding site separate from its active site.
  • Edc1p and Edc2p directly modulate decapping enzyme activity.