Preferred in vivo ubiquitination sites
| Autor: | Hidde L. Ploegh, Andre Catic, George M. Church, Cal Collins |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Statistics and Probability
Saccharomyces cerevisiae Proteins Adjuvant chemotherapy Saccharomyces cerevisiae Amino Acid Motifs Molecular Conformation Computational biology Ubiquitin-Activating Enzymes Biochemistry Substrate Specificity Structure-Activity Relationship Ubiquitin In vivo Sequence Analysis Protein Amino Acid Sequence Molecular Biology chemistry.chemical_classification Binding Sites biology Sequence Homology Amino Acid biology.organism_classification Computer Science Applications Amino acid Ubiquitin ligase Enzyme Activation Computational Mathematics Computational Theory and Mathematics chemistry biology.protein Protein Binding |
| Zdroj: | Bioinformatics (Oxford, England). 20(18) |
| ISSN: | 1367-4803 |
| Popis: | Motivation: The conjugation of ubiquitin to target molecules involves several enzymatic steps. Little is known about the specificity of ubiquitination. How E3 ligases select their substrate and which lysines are targeted for ubiquitin conjugation is largely an enigma. The object of this study is to identify preferred ubiquitination sites. Genetic approaches to study this question have proven difficult, because of the redundancy of ligases and the lack of strictly required motifs. However, a better understanding of acceptor site selection could help to predict ubiquitination sites and clarify yet unsolved structure–function relationships of the transfer reaction. Results: In an effort to define preferences for ubiquitination, we systematically analyzed structure and sequence of 135 known ubiquitination sites in 95 proteins in Saccharomyces cerevisiae. The results show clear structural preferences for ubiquitin ligation to target proteins, and compartment-specific amino acid patterns in close proximity to the modified side chain. Supplementary information: http://www.people.fas.harvard.edu/~catic |
| Databáze: | OpenAIRE |
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