Structure and Biochemistry of RsrI Methyltransferase

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Thomas, Chad Baldo

Contributors dc:contributor

• Gumport, Richard I.

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3101981

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84801