Carnegie Mellon University

Friday, November 6, 2015

Salini Konikkat

Salini Konikkat Wins Best Poster Award at Rustbelt RNA Meeting

Salini Konikkat was awarded a best poster award at the 2015 Rustbelt RNA meeting held in Sandusky, Ohio on October 23rd – 24th. RNA researchers from all over the region participated in the two days of exhibition, with six sessions of oral and poster presentations. Out of 146 posters presented at the meeting, Konikkat received one of only four best poster awards.

“The Rustbelt meeting is a wonderful opportunity to familiarize ourselves with the diverse research and discoveries in the RNA field, and also a great place to network,” said Konikkat, a graduate student in the Woolford lab.

Konikkat’s research focuses on how cells build ribosomes, the complex RNA-protein molecular nanomachines that catalyze protein synthesis in all cells. The Woolford lab studies the assembly of the 60S subunit of ribosomes, using baker’s yeast, S. cerevisiae, as a model organism.

“Yeast is an excellent model system since a wide variety of clever and cost-efficient assays [genetic, biochemical, and proteomic] can be employed to study this process,” Konikkat said.

Her poster, “Being present is a big part of any job, but not the only one: Multiple roles of the trans-acting Nop7-subcomplex in the assembly of yeast ribosomal 60S subunits”, presents Konikkat’s work in the investigation of how a group of three assembly factors, called the Nop7-subcomplex, help to build ribosomes via their interactions with proteins and RNA in ribosome precursor particles (pre-ribosomes).

To understand the importance of the interactions among Nop7, Erb1, and Ytm1, Konikkat constructed and assayed mutations in Erb1 predicted to disrupt its interactions with Nop7 and Ytm1. These new mutants revealed more functions for the Nop7 subcomplex than evident from the depletions. Depletion showed that in early stages of ribosome assembly, the Nop7-subcomplex proteins are required to assemble a specific neighborhood surrounding the polypeptide exit tunnel of the large subunit. In the more targeted Erb1 mutants predicted to disrupt Erb1 binding to Nop7, later steps in assembly are perturbed.

At present, Konikkat is using these mutants to study how the Nop7-subcomplex facilitates remodeling of RNA structure and recruitment of proteins in the pre-ribosomes.