Ann Arbor Times

On November 28, 2024, an international team of scientists, including researchers from the University of Michigan, published findings in the journal Science that reveal a structural link crucial for initiating protein synthesis in bacteria. The study focuses on how ribosomes are recruited to mRNA during transcription by RNA polymerase (RNAP).

Albert Weixlbaumer from the Institute of Genetics and Molecular and Cellular Biology at the University of Strasbourg explained, “Understanding how the ribosome captures or ‘recruits’ the mRNA is a prerequisite for everything that comes after.” The research team discovered that RNAP uses two anchors to secure ribosomes, ensuring effective protein synthesis initiation.

The study holds potential for developing new antibiotics targeting these pathways in bacterial protein synthesis. U-M senior scientist Adrien Chauvier noted, “We could target this interface... with a compound that interferes with the recruitment or stability of the complex.”

Researchers employed cryo-electron microscopy (cryo-EM) and other technologies to visualize these processes. Chauvier and Nils Walter used advanced fluorescence microscopes to analyze kinetics. They observed efficient binding of mRNA to ribosomal subunit 30S when ribosomal protein bS1 was present.

The study also highlighted an alternative pathway for mRNA delivery involving transcription factor NusG or its paralog RfaH. Huma Rahil and Michael Webster co-led this collaborative effort.