Year of Award

2015

Document Type

Dissertation - Campus Access Only

Degree Type

Doctor of Philosophy (PhD)

Degree Name

Chemistry

Department or School/College

Department of Chemistry and Biochemistry

Committee Chair

Klara Briknarova

Commitee Members

Bruce Bowler, Sandy Ross, Stephen Sprang, Holly Thompson

Keywords

NMR, PR domain, Protein

Publisher

The University of Montana

Abstract

Members of the PRDM protein family play important roles in stem cells and cellular differentiations. Several PRDM proteins have also been related to cancer. The PRDM proteins affect cellular differentiation by regulating gene transcription, but the underlying molecular mechanism is not yet clear. Herein, we tried to address this question by studying the molecular basis of the proposed histone methyltransferase activity of several PRDM proteins, as well as the interactions between PRDM proteins and other nuclear proteins. By using NMR spectroscopy and other biochemistry techniques, we found that, except for PRDM9, all the other PRDM proteins bind substrate and cofactors only with very low affinities, and mediate histone methyltransferase inefficiently by themselves. Therefore, the PRDM proteins might require interactions with other unknown macromolecules to exert their functions.

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© Copyright 2015 Yizhi Sun