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

Mediator-nucleosome interaction.

Y Lorch1, J Beve, C M Gustafsson

  • 1Department of Structural Biology, Stanford School of Medicine, Stanford, California 94305, USA.

Molecular Cell
|August 19, 2000
PubMed
Summary
This summary is machine-generated.

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

Analysis of the Candida albicans Phosphoproteome.

Eukaryotic cell·2015
Same author

The molecular basis of eucaryotic transcription.

Cell death and differentiation·2007
Same author

Bronchoalveolar neutrophils, interferon gamma-inducible protein 10 and interleukin-7 in AIDS-associated tuberculosis.

Clinical and experimental immunology·2007
Same author

The eukaryotic gene transcription machinery.

Biological chemistry·2001
Same author

Quantitation of the RNA polymerase II transcription machinery in yeast.

The Journal of biological chemistry·2001
Same author

Analysis of Schizosaccharomyces pombe mediator reveals a set of essential subunits conserved between yeast and metazoan cells.

Proceedings of the National Academy of Sciences of the United States of America·2001
Same journal

ChAHP silences SINE retrotransposons by inhibiting TFIIIB recruitment.

Molecular cell·2026
Same journal

Remodeling activity of ChAHP restricts transcription factor access to chromatin.

Molecular cell·2026
Same journal

Cryo-EM structure of soluble VPS13C suggests its regulation by a conformational switch and by calmodulin.

Molecular cell·2026
Same journal

HDAC5 depletion promotes hyper-acetylation of FOXA1 and potentiates HIF1α transcriptional activation in pancreatic cancer.

Molecular cell·2026
Same journal

Thyroid cancer-associated EZH1 Q571R mutation drives chromatin compaction and H3K27me3 invasion into active chromatin.

Molecular cell·2026
Same journal

Genome-wide rotational and translational phasing of nucleosomes with human transcription factors.

Molecular cell·2026
See all related articles

The Mediator complex regulates transcription and acetylates histones. Researchers identified the Nut1 subunit as responsible for this histone acetyltransferase (HAT) activity using multiple assays.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • Mediator is a crucial multiprotein complex regulating RNA polymerase II transcription.
  • Mediator interacts with nucleosomes and possesses histone acetyltransferase (HAT) activity.
  • The specific subunit responsible for Mediator's HAT activity was previously unidentified.

Purpose of the Study:

  • To identify the specific subunit of the Mediator complex responsible for its histone acetyltransferase (HAT) activity.
  • To characterize the HAT activity associated with the identified subunit.

Main Methods:

  • Performed "in-gel" histone acetyltransferase assays.
  • Conducted sequence alignment of the identified subunit against known acetyltransferase families.
  • Expressed and purified recombinant Nut1 protein for activity validation.

Related Experiment Videos

Main Results:

  • An "in-gel" HAT assay identified a single band corresponding to the Nut1 subunit.
  • Sequence analysis revealed significant similarity between Nut1 and the GCN5-related N-acetyltransferase superfamily.
  • Recombinant Nut1 protein demonstrated HAT activity in vitro.

Conclusions:

  • The Nut1 subunit is responsible for the histone acetyltransferase activity of the Mediator complex.
  • Nut1's HAT activity is conserved within the GCN5-related N-acetyltransferase superfamily.
  • These findings elucidate a key component of transcriptional regulation by Mediator.