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Universal Stress Proteins Associated with Glycolysis in Bacteria

Undergraduate #96
Discipline: Biological Sciences
Subcategory: Genetics

Abraham DaSilvio - Bethune-Cookman University
Co-Author(s): Raphael Isokpehi, Bethune-Cookman University, Daytona Beach, FL



Hypothesis: Through gene neighborhood analysis, we can possibly identify the biological process associations of the universal stress proteins and phosphatase enzymes. Importance: USP genes was discovered in E.coli, and have been found in both gram-negative, and gram-positive bacteria as well as in plants and fungi. Universal stress proteins respond to diverse habitat-related conditions that could adversely affect the survival of an organism. Identification of the functions of USP proteins could lead to new treatment options, antibiotics etc. for bacterial infections and diseases caused by pathogenic bacteria. Methods: A set of 30 universal stress proteins with a neighboring gene annotated with phosphatase were analyzed for operon arrangements and functional annotation. A three-digit transcription direction code was constructed for USP genes to in order to document the transcription direction of the adjacent genes relative to the gene encoding the universal stress protein domain. The middle digit of the binary code was always assigned “1″. If the adjacent gene is on same strand a “1” was assigned; otherwise a “0” was assigned. Therefore, the following binary codes were possible: 010, 110, 011, and 111. Controls: N/A Results: The findings from the analysis included a subset of USP genes on the same operon as genes for enolase and manganesedependent inorganic pyrophosphatase, in genomes of: Enterobacter, Erwinia, Pantoea, Serratia, and Edwardsiella. Conclusions and future research questions: Altogether, we have determined that glycolysis is a biological process where a universal stress protein is associated with a gene for phosphatase enzyme. Future research could investigate the influence of universal stress proteins in the regulation of glycolysis and the metabolism of adenosine triphosphate (ATP).

Not Submitted

Funder Acknowledgement(s): Targeted Infusion Project: Developing Quantitative Expertise in the Undergraduate Biology Curriculum (QEUBiC) [1435186]

Faculty Advisor: Raphael Isokpehi, isokpehir@cookman.edu

Role: I was given a dataset of 30 bacteria. I analyzed transcription units of the organisms in the dataset for operon arrangements and functional annotations. I then found a subset of USP genes on the same operon as genes for enolase and manganesedependent inorganic pyrophosphatase, in genomes of: Enterobacter, Erwinia, Pantoea, Serratia, and Edwardsiella. Since enolase and pyrophosphatase are both involved in Glycolysis, I then made my conclusion.

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This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.

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