Jaro L. Schmitt

The paper shows that the ribosome coordinates folding and assembly of a complex protein to enable efficient biogenesis.

This study investigates co-translational assembly of homomeric proteins, showing that PheA in E. coli primarily assembles via trans-assembly across neighboring mRNAs.

The paper reveals a temporal control mechanism driven by coupled ribosomes that enables the formation of intertwined protein dimers by bypassing closed monomeric states.

The paper shows co-translational ribosome pairing enables the formation of coiled-coil homodimers from misfolding-prone subunits through chaperone-like interactions between nascent chains.