Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization
- 13 May 2011
- journal article
- review article
- Published by IOP Publishing in Physical Biology
- Vol. 8 (3), 035007
- https://doi.org/10.1088/1478-3975/8/3/035007
Abstract
Many soluble and membrane proteins form homooligomeric complexes in a cell which are responsible for the diversity and specificity of many pathways, may mediate and regulate gene expression, activity of enzymes, ion channels, receptors, and cell adhesion processes. The evolutionary and physical mechanisms of oligomerization are very diverse and its general principles have not yet been formulated. Homooligomeric states may be conserved within certain protein subfamilies and might be important in providing specificity to certain substrates while minimizing interactions with other unwanted partners. Moreover, recent studies have led to a greater awareness that transitions between different oligomeric states may regulate protein activity and provide the switch between different pathways. In this paper we summarize the biological importance of homooligomeric assemblies, physico-chemical properties of their interfaces, experimental and computational methods for their identification and prediction. We particularly focus on homooligomer evolution and describe the mechanisms to develop new specificities through the formation of different homooligomeric complexes. Finally, we discuss the possible role of oligomeric transitions in the regulation of protein activity and compile a set of experimental examples with such regulatory mechanisms.Keywords
This publication has 89 references indexed in Scilit:
- Functional States of Homooligomers: Insights from the Evolution of GlycosyltransferasesJournal of Molecular Biology, 2010
- Dimer–monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transferProtein Science, 2010
- Evolution of Protein Binding Modes in HomooligomersJournal of Molecular Biology, 2010
- Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffoldProtein Science, 2009
- Protein acrobatics in pairs—dimerization via domain swappingCurrent Opinion in Structural Biology, 2009
- Built-in loops allow versatility in domain–domain interactions: Lessons from self-interacting domainsProceedings of the National Academy of Sciences of the United States of America, 2008
- Assembly reflects evolution of protein complexesNature, 2008
- Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene productsProceedings of the National Academy of Sciences of the United States of America, 2008
- Inference of Macromolecular Assemblies from Crystalline StateJournal of Molecular Biology, 2007
- Structural Similarity Enhances Interaction Propensity of ProteinsJournal of Molecular Biology, 2007