Protein stickiness, rather than number of functional protein-protein interactions, predicts expression noise and plasticity in yeast
Affiliation
Present address: Ecology & Evolutionary Biology, University of Arizona, 1041 E Lowell St, Tucson, AZ, 85721, USAPresent address: Bioengineering, University of Washington, 3720 15th Ave NE, Seattle, WA, 98195, USA
Issue Date
2012Keywords
Protein-protein interaction networksStochastic gene expression
Evolutionary constraint
Correlomics
Cooperativity
Phenotypic plasticity
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BioMed CentralCitation
Brettner and Masel BMC Systems Biology 2012, 6:128 http://www.biomedcentral.com/1752-0509/6/128Journal
BMC Systems BiologyRights
© 2012 Brettner and Masel; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0).Collection Information
This item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.Abstract
BACKGROUND:A hub protein is one that interacts with many functional partners. The annotation of hub proteins, or more generally the protein-protein interaction "degree" of each gene, requires quality genome-wide data. Data obtained using yeast two-hybrid methods contain many false positive interactions between proteins that rarely encounter each other in living cells, and such data have fallen out of favor.RESULTS:We find that protein "stickiness", measured as network degree in ostensibly low quality yeast two-hybrid data, is a more predictive genomic metric than the number of functional protein-protein interactions, as assessed by supposedly higher quality high throughput affinity capture mass spectrometry data. In the yeast Saccharomyces cerevisiae, a protein's high stickiness, but not its high number of functional interactions, predicts low stochastic noise in gene expression, low plasticity of gene expression across different environments, and high probability of forming a homo-oligomer. Our results are robust to a multiple regression analysis correcting for other known predictors including protein abundance, presence of a TATA box and whether a gene is essential. Once the higher stickiness of homo-oligomers is controlled for, we find that homo-oligomers have noisier and more plastic gene expression than other proteins, consistent with a role for homo-oligomerization in mediating robustness.CONCLUSIONS:Our work validates use of the number of yeast two-hybrid interactions as a metric for protein stickiness. Sticky proteins exhibit low stochastic noise in gene expression, and low plasticity in expression across different environments.EISSN
1752-0509Version
Final published versionAdditional Links
http://www.biomedcentral.com/1752-0509/6/128ae974a485f413a2113503eed53cd6c53
10.1186/1752-0509-6-128
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Except where otherwise noted, this item's license is described as © 2012 Brettner and Masel; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0).
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