Faculty Advisor

Adams, David S.

Abstract

Histones associate with DNA to make an octomer structure. In vitro assembly of the octomer would greatly facilitate its functional analysis, but this has not yet been achieved. A recently cloned yeast gene, CSE4, encodes a novel histone Cse4 that is thought to bind to specific DNA sequences to induce centromere formation. Cells lacking Cse4 cannot proceed through the cell cycle. The purpose of this MQP was to express in E. coli, for the first time, this new histone Cse4, as well as histones H2A, H2B, H3, and H4. Production levels were monitored by SDS-PAGE. Successful expression of all five histones was achieved, H2A and H2B were found to be soluble products, while H3, H4 and Cse4 were insoluble. The data represents the first production of S. cerevisiae histones H4 and Cse4 in an E. coli expression system. Further work must be done in order to construct the histone octamer in vitro.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2000

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Biology and Biotechnology

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