Creating Unique 3-D Printed Molecular Models to Explain the Role of HigB Toxin in Cleaving Ribosome-Bound mRNA
Abstract
The CREST (Connecting Researchers, Educators, and STudents) team at Nova Southeastern University created two physical models depicting the mechanism of endonuclease cleavage by the HigB protein, as described in the literature. Details of the HigB-ribosome complex and its residues for mRNA cleavage were found in the Protein Data Bank file, 4ZSN, and imported into Jmol, a protein visualization software. Specific program commands were developed to manipulate the original file into a format that was later 3D-printed. The models highlight the small ribosomal subunit, ribosomal proteins, tRNA, rRNA, the mRNA strand, and HigB protein along with its residues involved in mRNA cleavage. The N and C termini of the HigB were also indicated. HigB is part of a larger type II toxin (HigB) - antitoxin (HigA) system that cleaves ribosome-bound mRNAs in response to stress. Several bacteria use this mechanism, including Escherichia coli, Pseudomonas aeruginosa, and Proteus vulgaris. Chemical or physical stressors lead to antitoxin (HigA) degradation that releases HigB from the ribosome, inhibiting mRNA cleavage. HigB is of clinical interest due to its importance in mRNA recognition and cleavage in bacteria, thus affecting their survival in a variety of conditions possibly including antibiotics. These 3-D molecular models can be used to explain how ribosome-dependent proteins (HigB) target ribosomebound mRNAs in bacterial systems and allow students to actively engage in understanding the complex process of endonuclease cleavage. This work was funded in part by NSF-DUE 1725940 for the CREST project.
Faculty Sponsors
Dr. Emily Schmitt Lavin
Project Type
Event
Location
Alvin Shermany Library
Start Date
4-5-2019 1:00 PM
End Date
4-5-2019 5:00 PM
Creating Unique 3-D Printed Molecular Models to Explain the Role of HigB Toxin in Cleaving Ribosome-Bound mRNA
Alvin Shermany Library
The CREST (Connecting Researchers, Educators, and STudents) team at Nova Southeastern University created two physical models depicting the mechanism of endonuclease cleavage by the HigB protein, as described in the literature. Details of the HigB-ribosome complex and its residues for mRNA cleavage were found in the Protein Data Bank file, 4ZSN, and imported into Jmol, a protein visualization software. Specific program commands were developed to manipulate the original file into a format that was later 3D-printed. The models highlight the small ribosomal subunit, ribosomal proteins, tRNA, rRNA, the mRNA strand, and HigB protein along with its residues involved in mRNA cleavage. The N and C termini of the HigB were also indicated. HigB is part of a larger type II toxin (HigB) - antitoxin (HigA) system that cleaves ribosome-bound mRNAs in response to stress. Several bacteria use this mechanism, including Escherichia coli, Pseudomonas aeruginosa, and Proteus vulgaris. Chemical or physical stressors lead to antitoxin (HigA) degradation that releases HigB from the ribosome, inhibiting mRNA cleavage. HigB is of clinical interest due to its importance in mRNA recognition and cleavage in bacteria, thus affecting their survival in a variety of conditions possibly including antibiotics. These 3-D molecular models can be used to explain how ribosome-dependent proteins (HigB) target ribosomebound mRNAs in bacterial systems and allow students to actively engage in understanding the complex process of endonuclease cleavage. This work was funded in part by NSF-DUE 1725940 for the CREST project.
