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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Covalently Linked Protein Regulators

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These groups modify specific amino acids in a protein.

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Related Experiment Video

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Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
09:05

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

SCUD: Saccharomyces cerevisiae ubiquitination database.

Won-Chul Lee1, Minho Lee, Jin Woo Jung

  • 1Department of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea. cleariv@kaist.ac.kr

BMC Genomics
|September 25, 2008
PubMed
Summary

This study introduces SCUD, a comprehensive database detailing the ubiquitination system in Saccharomyces cerevisiae (Baker's yeast). It catalogs enzymes and substrates, aiding research into ubiquitination pathways.

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Published on: May 3, 2015

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Systems Biology

Background:

  • Ubiquitination is a critical post-translational modification regulating numerous biological processes.
  • A genomewide understanding of ubiquitination systems is essential for species-specific research.

Purpose of the Study:

  • To develop a comprehensive, web-based database for the yeast ubiquitination system.
  • To systematically catalog ubiquitination enzymes and their substrates in Saccharomyces cerevisiae.

Main Methods:

  • Searched for all known yeast ubiquitination enzymes (E1, E2, E3, deubiquitination enzymes).
  • Collected ubiquitinated substrates through literature review.
  • Classified E3 and deubiquitination enzymes by domains and functions.
  • Interconnected enzyme and substrate information via hyperlinks.

Main Results:

  • Identified 42 distinct E3 enzymes, categorized into classes and subclasses.
  • Cataloged 940 ubiquitinated substrates, including mutant forms.
  • Developed a user-friendly database (SCUD) with interconnected data.

Conclusions:

  • SCUD provides a comprehensive representation of the yeast ubiquitination system.
  • The database is designed for easy expansion with new experimental data.
  • SCUD is a valuable resource for studying ubiquitination in yeast and potentially other organisms.