One ring (or two) to hold them all – on the structure and function of protein nanotubes
- 23 June 2015
- journal article
- review article
- Published by Wiley in The FEBS Journal
- Vol. 282 (15), 2827-2845
- https://doi.org/10.1111/febs.13336
Abstract
Understanding the structural determinants relevant to the formation of supramolecular assemblies of homo-oligomeric proteins is a traditional and central scope of structural biology. The knowledge thus gained is crucial both to infer their physiological function and to exploit their architecture for bionanomaterials design. Protein nanotubes made by one-dimensional arrays of homo-oligomers can be generated by either a commutative mechanism, yielding an 'open' structure (e.g. actin), or a noncommutative mechanism, whereby the final structure is formed by hierarchical self-assembly of intermediate 'closed' structures. Examples of the latter process are poorly described and the rules by which they assemble have not been unequivocally defined. We have collected and investigated examples of homo-oligomeric circular arrangements that form one-dimensional filaments of stacked rings by the noncommutative mechanism in vivo and in vitro. Based on their quaternary structure, circular arrangements of protein subunits can be subdivided into two groups that we term Rings of Dimers (e.g. peroxiredoxin and stable protein 1) and Dimers of Rings (e.g. thermosome/rosettasome), depending on the sub-structures that can be identified within the assembly (and, in some cases, populated in solution under selected experimental conditions). Structural analysis allowed us to identify the determinants by which ring-like molecular chaperones form filamentous-like assemblies and to formulate a novel hypothesis by which nanotube assembly, molecular chaperone activity and macromolecular crowding may be interconnected.Keywords
Funding Information
- Sapienza Università di Roma
This publication has 67 references indexed in Scilit:
- Protein misinteraction avoidance causes highly expressed proteins to evolve slowlyProceedings of the National Academy of Sciences of the United States of America, 2012
- Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys PeroxiredoxinStructure, 2012
- Glutathionylation of Peroxiredoxin I Induces Decamer to Dimers Dissociation with Concomitant Loss of Chaperone ActivityBiochemistry, 2011
- Negative staining and cryo-negative staining of macromolecules and viruses for TEMMicron, 2011
- Crystal Structure of Group II Chaperonin in the Open StateStructure, 2010
- Typical 2‐Cys peroxiredoxins – structures, mechanisms and functionsThe FEBS Journal, 2009
- In vitro self-assembly of tailorable nanotubes from a simple protein building blockProceedings of the National Academy of Sciences of the United States of America, 2008
- Molecular crowding enhances native structure and stability of α/β protein flavodoxinProceedings of the National Academy of Sciences of the United States of America, 2007
- Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recoveryThe Journal of cell biology, 2006
- Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteinsNature Biotechnology, 2004