Investigation of Arc Protein Selective Binding to Arc 5' UTR mRNA Motif

Access Restricted

Access to this document is restricted. Some items have been embargoed at the request of the author, but will be made publicly available after the "No Access Until" date.

During the embargo period, you may request access to the item by clicking the link to the restricted file(s) and completing the request form. If we have contact information for a Cornell author, we will contact the author and request permission to provide access. If we do not have contact information for a Cornell author, or the author denies or does not respond to our inquiry, we will not be able to provide access. For more information, review our policies for restricted content.

No Access Until

Permanent Link(s)

Other Titles



Arc is a repurposed retrotransposon Gag protein that transports mRNA between neurons via assembling into virus-like capsids. An Arc homolog, the HIV Gag, can selectively package the 5’ untranslated region (UTR) of its own genome RNA, leading to more efficient capsid assembly than other abundant host cytoplasmic RNAs. There is currently limited understanding on the mRNA selection mechanism during Arc capsid assembly. Investigating this mechanism can provide insight into Arc’s role in neurological function and impact within neurodegenerative diseases as well as for utilizing Arc as a potential delivery vehicle for therapeutic applications. Here, we investigate any preference that Arc protein potentially has towards binding the Arc 5’ UTR mRNA motif over other mRNA sequences. Dynamic light scattering (DLS) measurements and atomic force microscopy (AFM) confirmed in vitro Arc capsid assembly encapsulates any mRNA that are prominently present within the environment. A custom-made surface plasmon resonance (SPR) biosensor allowed for an in-depth study of biomolecular interactions between mRNA and Arc. The SPR biosensor results showcased Arc’s ability to nonspecifically bind to any mRNA sequence. Furthermore, it confirmed the existence of a selective mRNA binding site on Arc’s CA domain to the Arc 5’ UTR mRNA sequence and how this selective interaction can initiate Arc multimerization for capsomere assembly.

Journal / Series

Volume & Issue


96 pages


Date Issued




activity-regulated cytoskeleton-associated protein; capsid assembly; RNA - protein interaction; surface plasmon resonance


Effective Date

Expiration Date




Union Local


Number of Workers

Committee Chair

Yu, Qiuming

Committee Co-Chair

Committee Member

Yang, Rong

Degree Discipline

Chemical Engineering

Degree Name

M.S., Chemical Engineering

Degree Level

Master of Science

Related Version

Related DOI

Related To

Related Part

Based on Related Item

Has Other Format(s)

Part of Related Item

Related To

Related Publication(s)

Link(s) to Related Publication(s)


Link(s) to Reference(s)

Previously Published As

Government Document




Other Identifiers


Attribution 4.0 International


dissertation or thesis

Accessibility Feature

Accessibility Hazard

Accessibility Summary

Link(s) to Catalog Record