Literature DB >> 25473139

SELECTIVE ADVANTAGE OF RECOMBINATION IN EVOLVING PROTEIN POPULATIONS: A LATTICE MODEL STUDY.

Paul D Williams1, David D Pollock2, Richard A Goldstein3.   

Abstract

Recent research has attempted to clarify the contributions of several mutational processes, such as substitutions or homologous recombination. Simplistic, tractable protein models, which determine the compact native structure phenotype from the sequence genotype, are well-suited to such studies. In this paper, we use a lattice-protein model to examine the effects of point mutation and homologous recombination on evolving populations of proteins. We find that while the majority of mutation and recombination events are neutral or deleterious, recombination is far more likely to be beneficial. This results in a faster increase in fitness during evolution, although the final fitness level is not significantly changed. This transient advantage provides an evolutionary advantage to subpopulations that undergo recombination, allowing fixation of recombination to occur in the population.

Entities:  

Keywords:  homologous protein recombination; introns; lattice-protein

Year:  2006        PMID: 25473139      PMCID: PMC4249953          DOI: 10.1142/S0129183106008959

Source DB:  PubMed          Journal:  Int J Mod Phys C        ISSN: 0129-1831            Impact factor:   1.176


  20 in total

1.  Modeling evolutionary landscapes: mutational stability, topology, and superfunnels in sequence space.

Authors:  E Bornberg-Bauer; H S Chan
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-14       Impact factor: 11.205

2.  The evolutionary landscape of functional model proteins.

Authors:  J D Hirst
Journal:  Protein Eng       Date:  1999-09

3.  A hierarchical approach to protein molecular evolution.

Authors:  L D Bogarad; M W Deem
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

4.  Why are proteins so robust to site mutations?

Authors:  Darin M Taverna; Richard A Goldstein
Journal:  J Mol Biol       Date:  2002-01-18       Impact factor: 5.469

5.  Evolution of functionality in lattice proteins.

Authors:  P D Williams; D D Pollock; R A Goldstein
Journal:  J Mol Graph Model       Date:  2001       Impact factor: 2.518

6.  Evolution of evolvability via adaptation of mutation rates.

Authors:  Mark A Bedau; Norman H Packard
Journal:  Biosystems       Date:  2003-05       Impact factor: 1.973

7.  Fitness-associated recombination on rugged adaptive landscapes.

Authors:  L Hadany; T Beker
Journal:  J Evol Biol       Date:  2003-09       Impact factor: 2.411

8.  Roles of mutation and recombination in the evolution of protein thermodynamics.

Authors:  Yu Xia; Michael Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-29       Impact factor: 11.205

9.  Stability and the evolvability of function in a model protein.

Authors:  Jesse D Bloom; Claus O Wilke; Frances H Arnold; Christoph Adami
Journal:  Biophys J       Date:  2004-05       Impact factor: 4.033

10.  Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution.

Authors:  Yu Xia; Michael Levitt
Journal:  Proteins       Date:  2004-04-01
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