Investigation of Caenorhabditis elegans RNA Helicase A Protein Binding with a Yeast 2-Hybrid Assay

Carly Summers

Date of Award

2005

Document Type

Thesis

Degree Name

Bachelors

Department

Natural Sciences

First Advisor

Walstrom, Katherine

Keywords

Yeast 2-Hybrid, Helicase, Protein

Area of Concentration

Biochemistry

Abstract

RNA helicase A (RHA) is a highly conserved helicase protein with established roles in nucleic acid binding and transcription regulation. In order to better understand the function of RHA in the model organism C. elegans, a yeast 2-hybrid assay was performed to identify proteins that interact with RHA-1, the C. elegans form of RHA. A p-ACT RB2 randomprimed C. elegans cDNA library was used to perform this screen within the yeast strain PJ69-4A. One protein in the screen was found to specifically interact with RHA-1. This protein is calnexin (CNX-1), a molecular chaperone currently thought to be localized to the endoplasmic reticulum. The probability and implications of a RHA 1/CNX-1 interaction are discussed in the context of the results of this experiment as well as literature related to the proteins of interest.

Rights

This bibliographic record is available under the Creative Commons CC0 public domain dedication. The New College of Florida, as creator of this bibliographic record, has waived all rights to it worldwide under copyright law, including all related and neighboring rights, to the extent allowed by law.

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