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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...

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A Reporter Based Cellular Assay for Monitoring Splicing Efficiency
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Published on: September 15, 2021

Structural characterization of human Uch37.

Sethe E Burgie1, Craig A Bingman, Ameet B Soni

  • 1Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison Wisconsin 53706-1544.

Proteins
|September 29, 2011
PubMed
Summary
This summary is machine-generated.

The study reveals the X-ray crystal structure of Uch37, a de-ubiquitylating enzyme crucial for development. This structural insight, along with corrected activity analyses, aids understanding of Uch37

Keywords:
UCH-L5deubiquitylating enzymesproteasomeprotein assemblyubiquitinubiquitin C-terminal hydrolase

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Uch37 is a de-ubiquitylating enzyme essential for metazoan development.
  • It functions with the 26S proteasome through Rpn13.

Purpose of the Study:

  • To determine the X-ray crystal structure of full-length human Uch37.
  • To characterize Uch37's oligomeric state and activity.

Main Methods:

  • X-ray crystallography at 2.95 Å resolution.
  • Biochemical assays for activity characterization.

Main Results:

  • The crystal structure of full-length human Uch37 was determined.
  • The catalytic domain resembles other UCH enzymes.
  • A unique, elongated, helical C-terminal extension with coiled coil interactions was observed.
  • A systematic error in previous Uch37 activity analyses was identified.

Conclusions:

  • The determined structure provides a foundation for understanding Uch37's functions.
  • Structural and activity data will facilitate further research into Uch37's roles.