Christine Mayr, Professor of Biochemistry & Molecular Biology; and Professor of Computational Biology & Medicine, at Memorial Sloan Kettering Cancer Center, and at Weill Cornell Medical College, will give a talk titled, "Protein folding regulated by mRNA 3′UTRs acting as RNA-based chaperones."

This seminar will also be available by Zoom. Zoom link: https://gc-cuny.zoom.us/j/91607074885?pwd=3peeVNPa5kUJJ48m7lObDWLl3SQ1n… Meeting ID: 916 0707 4885. Passcode: ASRCccny.

Please note: 

* Full names must be used to be admitted to the Zoom meeting.

* The Zoom meeting will be closed and locked at 12:15 p.m., and no one will be able to enter the meeting after that time.

ABSTRACT

More than 2,700 human mRNA 3′UTRs have hundreds of highly conserved (HC) nucleotides, but their biological roles are unclear. A large fraction of mRNAs with highly conserved 3′UTRs encodes proteins with long intrinsically disordered regions (IDRs). For the tested candidates, we observed that these proteins are only fully active when translated from mRNA templates that include their 3′UTRs, raising the possibility of functional interactions between 3′UTRs and IDRs. Rather than affecting protein abundance or localization, we find that highly conserved 3′UTRs directly control protein activity through protein folding of IDR-containing proteins. Presence of the 3′UTR is required to prevent interference of hydrophobic clusters in the IDR with the folding of the structured domains of the mRNA-encoded protein. In addition to folding of individual proteins, we also observed that for some transcription factors 3′UTR-3′UTR interactions determine the co-folding of the mRNA-encoded proteins, thus generating stable heterodimers. Taken together, our work indicates that highly conserved 3′UTRs regulate protein activity in an abundance-independent manner, by controlling different co-translational protein folding pathways.