Abstract
Ubiquitylation is an important regulatory mechanism in the eukaryotic cell. A large volume of experimental data on protein ubiquitylation has been acquired in recent years. Particular ubiquitylated lysine residues were also identified. This allows us to analyze co-localization of ubiquitylation sites and functionally important protein domains, following the idea that ubiquitylation can directly affect protein functional activity. Computational analysis suggests that ubiquitylation can affect the functional activity of some proteins through direct steric effects. (1) Ubiquitylation can block protein functional domains/active site or cause accessibility limitations. It also (2) causes steric disturbances for homo-oligomerization and (3) influences heterologous protein interactions, impeding the binding of target protein with its partners. (4) Interaction with partner proteins can be disturbed by restricted conformational flexibility. Any of these effects will result in a decrease of target protein activity. Thus, we suggest a new “loss-of-function” mechanism of protein regulation by ubiquitylation.
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Chernorudskiy, A.L., Shorina, A.S., Garcia, A. et al. Evaluation of direct effects of protein ubiquitylation using computational analysis. BIOPHYSICS 51 (Suppl 1), 39–43 (2006). https://doi.org/10.1134/S0006350906070086
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DOI: https://doi.org/10.1134/S0006350906070086