Initial Biochemical and Structural Studies of Frequency-Interacting RNA Helicase, an Mtr4-like Protein from Neurospora crassa

Document Type

Presentation

Publication Date

4-10-2014

Faculty Mentor

Sean Johnson

Abstract

Frequency-interacting RNA-Helicase (FRH) from the fungal species Neurospora crassa is a key player in circadian rhythms and is predicted to mediate exosomal RNA degradation. The dual functionality of this helicase within two separate pathways is novel and unique to N. crassa. A related helicase, Mtr4 has been a long-term focus of the Johnson lab. FRH and Mtr4 are predicted to have significant structural and functional similarities. Comparing the two helicases will help elucidate the understanding of their functions within each system. In order to further understand FRH and how it compares to Mtr4, we have initiated biochemical and structural studies. As a first step, we have developed expression vectors for recombinant expression of full length and truncated FRH in E. coli. Expression protocols have been established, and a protein purification strategy for these two FRH constructs is currently under development.

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