Szostak notes that the final version of the enzyme they created is quite small and still not very stable, but it is a starting point to discovering additional strategies that may help improve its activity. The same mRNA-display technique can also identify enzymes that break down or otherwise modify their substrate molecules.
We hope our work on optimizing this enzyme will demonstrate that we can evolve catalysts with activity as good as that of naturally occurring enzymes, Szostak explains. Wed also like to determine the 3D structure of our new enzyme to understand how it binds to its relatively larger substrates and catalyzes the joining of the two RNA strands. The Alex Rich Distinguished Investigator in Molecular Biology at MGH, Szostak also is a professor of Genetics at Harvard Medical School, a Howard Hughes Medical Institute investigator and a member of the MGH Center for Computational and Integrative Biology. This study was supported by a grant from the NASA Astrobiology Institute, and Seeligs was supported in part by the Emmy Noether-Programm of the Deutsche Forschungsgemeinschaft.
'/>"/>
| Contact: Sue McGreevey smcgreevey@partners.org 617-724-2764 Massachusetts General Hospital Source:Eurekalert |