Matthieu Gagnon

2016 Regional Award Finalist — Post-Doc

Matthieu Gagnon

Current Position:
Associate Research Scientist

Institution:
Yale University

Discipline:
Biochemistry & Structural Biology

Recognized for: Providing insights into the function of multiple ribosomal protein factors and antimicrobial peptides and their roles in protein synthesis

Areas of Research Interest and Expertise:  Protein synthesis and regulation, ribosome structure, ribosomal RNA, mRNA translation, structural biology

Biography:

PhD, Biochemistry, University of Montreal
MSc, Biochemistry, University of Montreal
BSc, Biochemistry, University of Montreal

Dr. Gagnon studies protein synthesis, a process performed by the ribosome in all living organisms. The ribosome “reads” the messenger RNA and converts the genetic information into proteins.  During his PhD training with Dr. Steinberg at the University of Montreal in Canada, Dr. Gagnon performed both computational and experimental work.  Dr. Gagnon literally dissected the structure of the ribosome, taking apart all elements of ribosomal RNA.  He uncovered a new RNA structural motif found in many locations of the ribosome structure. Remarkably, the same RNA motif also fixes the transfer RNAs (tRNA) on the ribosome and is coordinating tRNA movement during protein synthesis.

To pursue his studies of protein synthesis, Dr. Gagnon joined the laboratory of Professor Thomas Steitz at Yale University. In collaboration with several colleagues, he established innovative crystallographic approaches to determine the atomic details of the ribosome bound with various ligands, such as rescue factors, antimicrobial peptides and translational GTPases. The multiple snapshots of ribosome complexes he obtained have provided important insights into how stalled ribosomes are being rescued, how GTPases promote key steps of proteins synthesis and how antimicrobial peptides could be used as new antibiotics capable of inhibiting protein synthesis in many pathogens.

“Protein synthesis and its regulation are essential for gene expression and dysfunction in translation results in numerous human diseases. My goal is to understand the molecular mechanisms by which gene expression is regulated at the level of translation by the ribosome itself and the numerous translation factors.”

Key Publications:

  1. Gagnon MG, Lin J, Steitz TA. Elongation factor 4 remodels the A-site tRNA on the ribosome. Proc. Natl. Acad. Sci. USA. 2016
  2. Gagnon MG, Roy RN, Lomakin IB, Florin T, Mankin AS, Steitz TA. Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res. 2016
  3. Gagnon MG, Lin J, Bulkley D, Steitz TA. Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science. 2014
  4. Gagnon MG, Seetharaman SV, Bulkley D, Steitz TA. Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science. 2012

Other Honors:

2008       Achievement Awards for Outstanding Research, University of Montreal, Canada
2003       Canada Graduate Scholarship, Natural Sciences and Engineering Research Council of Canada
2003       Fonds de la Recherche en Santé du Québec, Two-year Graduate Fellowship
2001       Achievement Award for Outstanding Master Research, Luigi Liberatore Fellowship, University of Montreal

In the Media:

Research in the News: Key worker in protein synthesis factory revealed. Yale News. August 7, 2014