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Protein robustness promotes evolutionary innovations on large evolutionary time-scales


Ferrada, E; Wagner, A (2008). Protein robustness promotes evolutionary innovations on large evolutionary time-scales. Proceedings of the Royal Society B: Biological Sciences, 275(1643):1595-1602.

Abstract

Recent laboratory experiments suggest that a molecule's ability to evolve neutrally is important for its ability to generate evolutionary innovations. In contrast to laboratory experiments, life unfolds on time-scales of billions of years. Here, we ask whether a molecule's ability to evolve neutrally-a measure of its robustness-facilitates evolutionary innovation also on these large time-scales. To this end, we use protein designability, the number of sequences that can adopt a given protein structure, as an estimate of the structure's ability to evolve neutrally. Based on two complementary measures of functional diversity-catalytic diversity and molecular functional diversity in gene ontology-we show that more robust proteins have a greater capacity to produce functional innovations. Significant associations among structural designability, folding rate and intrinsic disorder also exist, underlining the complex relationship of the structural factors that affect protein evolution.

Abstract

Recent laboratory experiments suggest that a molecule's ability to evolve neutrally is important for its ability to generate evolutionary innovations. In contrast to laboratory experiments, life unfolds on time-scales of billions of years. Here, we ask whether a molecule's ability to evolve neutrally-a measure of its robustness-facilitates evolutionary innovation also on these large time-scales. To this end, we use protein designability, the number of sequences that can adopt a given protein structure, as an estimate of the structure's ability to evolve neutrally. Based on two complementary measures of functional diversity-catalytic diversity and molecular functional diversity in gene ontology-we show that more robust proteins have a greater capacity to produce functional innovations. Significant associations among structural designability, folding rate and intrinsic disorder also exist, underlining the complex relationship of the structural factors that affect protein evolution.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry

Special Collections > SystemsX.ch
Special Collections > SystemsX.ch > Research, Technology and Development Projects > YeastX
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:July 2008
Deposited On:17 Sep 2008 12:59
Last Modified:06 Dec 2017 14:23
Publisher:Royal Society of London
ISSN:0962-8452
Free access at:PubMed ID. An embargo period may apply.
Publisher DOI:https://doi.org/10.1098/rspb.2007.1617
PubMed ID:18430649

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