Pehu Kohli

CcdA chaperones CcdB against irreversible misfolding and aggregation via a cotranslational folding mechanism

The paper shows that CcdA suppresses folding defects in CcdB mutants through cotranslational assembly, highlighting the importance of operon structure in protein complex formation.

The high mutational sensitivity of ccdA antitoxin is linked to codon optimality

The paper shows that ccdA antitoxin in E. coli is highly sensitive to mutations, including synonymous ones, due to codon usage and operonic context effects on translation efficiency.

Loss of function from widely distributed, synonymous mutations at single codons

The paper shows that synonymous mutations can cause loss of function by altering RNA structure and gene expression ratios, validated in multiple operons.