Structure and Biochemistry of RsrI Methyltransferase

125 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.Comparison of the dimer interface of M.RsrI with the recent M.MboII structure and sequence alignments allowed identification of a conserved dimerization motif. I disrupted the dimerization of M.RsrI by adding N-acetyl-phenylalanine as a competitive inhibitor and by mutation of a serine located in the dimer interface to an aspartate. Both methods resulted in inhibition of the enzyme activity, suggesting dimerization is important for enzyme activity.U of I OnlyRestricted to the U of I community idenfinitely during batch ingest of legacy ETD