D. Allan Drummond

Assistant Professor (Biochemistry and cell biology not elsewhere classified)

Chicago

Dr. Drummond is an Assistant Professor of Biochemistry & Molecular Biology and Human Genetics. The Drummond Lab (http://drummondlab.org) studies how cells respond to stress at the molecular level, focusing on formation and dissolution of large assemblies of proteins and RNA during and after stresses such as heat shock. Drummond's lab uses a wide range of techniques, including in vivo imaging, in vitro reconstitution and mechanistic biochemistry, quantitative proteomics, and molecular evolutionary analysis. Because many features of stress-triggered assembly processes are shared across eukaryotes, including humans, the group employs budding yeast, Saccharomyces cerevisiae, as a model organism.

Publications

A nutrient-driven tRNA modification alters translational fidelity and genome-wide protein coding across an animal genus DOI: 10.1371/journal.pbio.1002015
Estimating a structured covariance matrix from multi-lab measurements in high-throughput biology. DOI: 10.1080/01621459.2014.964404
Estimating selection on synonymous codon usage from noisy experimental data. DOI: 10.1093/molbev/mst051
Good codons, bad transcript: large reductions in gene expression and fitness arising from synonymous mutations in a key enzyme. DOI: 10.1093/molbev/mss273
Quantifying condition-dependent intracellular protein levels enables high-precision fitness estimates. PMID: 24086506
How infidelity creates a sticky situation. DOI: 10.1016/j.molcel.2012.11.024
Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. DOI: 10.1073/pnas.1017570108
Signatures of protein biophysics in coding sequence evolution. DOI: 10.1016/j.sbi.2010.03.004
The evolutionary consequences of erroneous protein synthesis. DOI: 10.1038/nrg2662
Protein evolution: innovative chaps. DOI: 10.1016/j.cub.2009.07.039
Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. DOI: 10.1016/j.cell.2008.05.042
Contact density affects protein evolutionary rate from bacteria to animals. DOI: 10.1007/s00239-008-9094-4
A diverse family of thermostable cytochrome P450s created by recombination of stabilizing fragments. DOI: 10.1038/nbt1333
Structural determinants of the rate of protein evolution in yeast. DOI: 10.1093/molbev/msl040
Population genetics of translational robustness. DOI: 10.1534/genetics.105.051300
A single determinant dominates the rate of yeast protein evolution. DOI: 10.1093/molbev/msj038
Predicting the tolerance of proteins to random amino acid substitution. DOI: 10.1529/biophysj.105.062125
Why highly expressed proteins evolve slowly. DOI: 10.1073/pnas.0504070102
Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. DOI: 10.1016/j.jmb.2005.05.023
On the conservative nature of intragenic recombination. DOI: 10.1073/pnas.0500729102
Thermodynamic prediction of protein neutrality. DOI: 10.1073/pnas.0406744102
Reversible, specific, active aggregates of endogenous proteins assemble upon heat stress. DOI: 10.1016/j.cell.2015.08.041

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Joshua A. Riback

D. Allan Drummond

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