Office of Undergraduate Research

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Emphasizing equitable and inclusive access to research opportunities, the University of Maryland's Office of Undergraduate Research (OUR) empowers undergraduates and faculty to engage and succeed in inquiry, creative activity, and scholarship. This collection includes materials shared by undergraduate researchers during OUR events. It also encompasses materials from Undergraduate Research Day 2020, Undergraduate Research Day 2021, and Undergraduate Research Day 2022, which were organized by the Maryland Center for Undergraduate Research.

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Author: search.filters.author.Baker, CharleySubject: search.filters.subject.AGNR

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    Identification of Clostridium Phage Endolysins with Novel Multimeric Genetic Sequences
    (2021) Bokil, Eesha; Baker, Charley; Nelson, Daniel; O'Hara, Jessica
    The endolysin CD27L is produced by the Clostridium phage phiCD27. This phage targets the bacteria and uses the endolysin’s enzymatic properties to lyse cells from within and release new replicated phages. Past studies have characterized the two domains of CD27L’s genetic sequence, the enzymatically active domain (EAD) at the N-terminus and the cell wall binding domain (CBD) at the C-terminus connected by a linker sequence. The gene sequence order is EAD-linker-CBD. A unique aspect of CD27L is its ability to form a multimeric enzymatic structure from these two domains where one EAD and multiple CBDs are present in one structure. This multimeric endolysin is formed from one gene, so translation of the one sequence uses two ribosome binding sites and two start codons. One ribosome binding site and start codon is before the EAD and the other in the linker sequence before the CBD. Our goal is to analyze the sequences of other Clostridium phage endolysins to find multimeric endolysins similar to CD27L. We are specifically looking for multiple ribosome binding sites with start codons or alternate start codons downstream in close proximity on one gene sequence.