Sigma Xi Poster Competition
Academic Level at Time of Presentation
Junior
Major
Chemistry
Minor
Biology
List all Project Mentors & Advisor(s)
Dr. Christopher Lennon
Presentation Format
Poster Presentation
Abstract/Description
Intervening proteins (inteins) are translated within host proteins and removed by protein splicing. Inteins are abundant in the microbial world and are often found within essential genes involved in DNA replications, recombination, and repair. Recent studies have made efforts to understand conditional proteins splicing, whereby intein removal and subsequent host protein activation is regulated by environmental factors. However, within the cellular context, factors influencing protein splicing are still largely unknown. In this work, we probe whether the chaperonin system GroEL/ES promotes protein splicing in vivo. Chaperonins, a family of chaperone proteins, help proteins fold under normal and stressed conditions. Here we demonstrate that GroEL appears to promote splicing of a DnaB intein from Mycobacterium smegmatis within an in vivo reporter. This reporter (KISR) requires splicing to provide resistance to the antibiotic kanamycin. Upon GroEL expression, survival of KISR-containing Escherichia coli cells drastically improves compared to an empty vector control. Importantly, GroEL expression does not increase survival of E. coli cells expressing the kanamycin resistance protein, KanR, lacking an intein. Our findings using our KISR reporter suggest that GroEL can promote protein splicing in vivo. Future work will probe whether GroEL expression directly promotes M. smegmatis DnaB intein splicing. If so, this would represent the first example of another protein increasing splicing of an intein containing protein.
Spring Scholars Week 2025
Sigma Xi Poster Competition
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Do Chaperones Promote Protein Splicing?
Intervening proteins (inteins) are translated within host proteins and removed by protein splicing. Inteins are abundant in the microbial world and are often found within essential genes involved in DNA replications, recombination, and repair. Recent studies have made efforts to understand conditional proteins splicing, whereby intein removal and subsequent host protein activation is regulated by environmental factors. However, within the cellular context, factors influencing protein splicing are still largely unknown. In this work, we probe whether the chaperonin system GroEL/ES promotes protein splicing in vivo. Chaperonins, a family of chaperone proteins, help proteins fold under normal and stressed conditions. Here we demonstrate that GroEL appears to promote splicing of a DnaB intein from Mycobacterium smegmatis within an in vivo reporter. This reporter (KISR) requires splicing to provide resistance to the antibiotic kanamycin. Upon GroEL expression, survival of KISR-containing Escherichia coli cells drastically improves compared to an empty vector control. Importantly, GroEL expression does not increase survival of E. coli cells expressing the kanamycin resistance protein, KanR, lacking an intein. Our findings using our KISR reporter suggest that GroEL can promote protein splicing in vivo. Future work will probe whether GroEL expression directly promotes M. smegmatis DnaB intein splicing. If so, this would represent the first example of another protein increasing splicing of an intein containing protein.