ArticleBiochemistry2010
Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Rheostat functional outcomes occur when substitutions are introduced at nonconserved positions that diverge with speciation.Protein science : a publication of the Protein Society · 2021Article
- The genotype-phenotype landscape of an allosteric protein.Molecular systems biology · 2021Article
- The strengths and limitations of using biolayer interferometry to monitor equilibrium titrations of biomolecules.Protein science : a publication of the Protein Society · 2020Article
- Experimental evolution and proximate mechanisms in biology.Synthetic and systems biotechnology · 2017Review
- Data on publications, structural analyses, and queries used to build and utilize the AlloRep database.Data in brief · 2016Article
- What Mutagenesis Can and Cannot Reveal About Allostery.Biophysical journal · 2016Review
- Article
- Environmental dependence of genetic constraint.PLoS genetics · 2013Article
- FRET studies of a landscape of Lac repressor-mediated DNA loops.Nucleic acids research · 2012Article
- Altering residues N125 and D149 impacts sugar effector binding and allosteric parameters in Escherichia coli lactose repressor.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The central region of the LacI N-subdomain monomer-monomer interface includes residues K84, V94, V95, V96, S97, and M98. The side chains of these residues line the β-strands at this interface and interact to create a network of hydrophobic, charged, and polar interactions that significantly rearranges in different functional states of LacI. Prior work showed that converting K84 to an apolar residue or converting V96 to an acidic residue impedes the allosteric response to inducer. Thus, we postulated that a disproportionate number of substitutions in this region of the monomer-monomer interface would alter the complex features of the LacI allosteric response. To explore this hypothesis, acidic, basic, polar, and apolar mutations were introduced at positions 94-98. Despite their varied locations along the β-strands that flank the interface, ∼70% of the mutations impact allosteric behavior, with the most significant effects found for charged substitutions. Of note, many of the LacI variants with minor functional impact exhibited altered stability to urea denaturation. The results confirm the critical role of amino acids 94-98 and indicate that this N-subdomain interface forms a primary pathway in LacI allosteric response.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.