Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

GroEL/S Overexpression Helps to Purge Deleterious Mutations and Reduce Genetic Diversity during Adaptive Protein Evolution.

Molecular biology and evolution - 2 Jun 2022

Iyengar Bharat Ravi, Wagner Andreas

Abstract excerpt

Chaperones are proteins that help other proteins fold. They also affect the adaptive evolution of their client proteins by buffering the effect of deleterious mutations and increasing the genetic diversity of evolving proteins. We study how the bacterial chaperone GroE (GroEL+GroES) affects the evolution of green fluorescent protein (GFP). To this end, we subjected GFP to multiple rounds of mutation and selection...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Chaperonin 60
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Heat-Shock Proteins

Share to Molecular Chaperones

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 35234895
DOI: 10.1093/molbev/msac047
PMCID: PMC9188349

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

GroEL/S Overexpression Helps to Purge Deleterious Mutations and Reduce Genetic Diversity during Adaptive Protein Evolution.PMID 35234895Read ↗

Fitness Trade-Offs Determine the Role of the Molecular Chaperonin GroEL in Buffering Mutations.Semantic proximity Read ↗

Bacterial Hsp90 predominantly buffers but does not potentiate the phenotypic effects of deleterious mutations during fluorescent protein evolution.Semantic proximity Read ↗

Low protein expression enhances phenotypic evolvability by intensifying selection on folding stability.Semantic proximity Read ↗

Evolutionary dynamics and structural consequences of de novo beneficial mutations and mutant lineages arising in a constant environment.Semantic proximity Read ↗

Mistranslation Reduces Mutation Load in Evolving Proteins through Negative Epistasis with DNA Mutations.Semantic proximity Read ↗

High-throughput characterization of mutations in genes that drive clonal evolution using multiplex adaptome capture sequencing.Semantic proximity Read ↗

Selection enhances protein evolvability by increasing mutational robustness and foldability.Semantic proximity Read ↗

GROEL/ES Buffers Entropic Traps in Folding Pathway during Evolution of a Model Substrate.Semantic proximity Read ↗

GroEL/ES buffering and compensatory mutations promote protein evolution by stabilizing folding intermediates.Semantic proximity Read ↗

Profiling the initial burst of beneficial genetic diversity in clonal cell populations to anticipate evolutionSemantic proximity Read ↗

Chaperonin overexpression promotes genetic variation and enzyme evolution.Semantic proximity Read ↗

Predicting the effect of mutations to investigate recent events of selection across 60,472 Escherichia coli strains.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.