Kyle Heard

The ribosome is a universally conserved ribonucleoprotein complex that translates the genetic code into protein synthesis. Recently improved CryoEM structures revealed a previously unmodeled isoaspartyl (isoAsp) modification on an encoded Asn within a 30S ribosomal protein. This unique ribosomal protein backbone modification of Asn into isoAsp inserts an additional methylene group into the backbone. My research investigates the biosynthetic origin of the metal-dependent enzyme that is responsible for catalyzing the isoAsp modification using a combination of structure-function and enzyme kinetics analyses. These studies will elucidate an enzymatic process conserved across all domains of life.