Environmental conditions modulate protein heterogeneity though transcriptional and translational stop codon miscoding by degradation

Romero Romero, M.L.*, Poehls, J., Kirilenko, A., Richter, D., Jumel, T., Shevchenko, A., & Toth-Petroczy, A.* (2024) Nat. Commun., 15(1), 4446.

We show that Stop Codon Readthrough—a ‘molecular typo’ where protein synthesis continues past a stop signal— is a driver of protein diversity under stress. This suggests a cross-talk between the environment and the biological flux of information that provides a rapid mechanism to adapt to changing conditions.

Active site center redesign protein stability preserving catalysis in thioredoxin

Romero Romero, M.L.*, Garcia Seisdedos, H., & Ibarra‐Molero, B. (2022) Protein Science, 31(9), e4417

By redesigning thioredoxin’s surface charge distribution to mimic the catalytic properties of a buried charged residue, we engineered a hyperstable variant with record thermal stability and enhanced activity, advancing protein engineering.

Simple yet functional Phosphate-loop proteins

Romero Romero, M.L., Yang, F., Lin, Y.R., Toth-Petroczy, A., Berezovsky, I.N., Goncearenco, A., Yang W., Wellner A., Kumar-Deshmukh F., Sharon M., Baker D., Varani G. & Tawfik, D.S. (2018) Proc Natl Acad Sci U S A., 115(51), E11943-E11950

We provide the first example of embedding a functional element into a de novo scaffold to generate a biochemically active protein

Functional proteins from short peptides: Dayhoff’s hypothesis turns 50

Romero Romero, M.L., Rabin, A., & Tawfik, D.S. (2016) Angew Chem Int Ed Engl., 55(52), 15966-15971

Fifty years after Dayhoff’s seminal paper, this work reinforces and validates her hypothesis, now forming a general model for the emergence of large, globular, and functional proteins from relatively short, simple peptides