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Electrostatic and hydrophobic interactions between ricin toxin a chain and the ribosome
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Zhou, Yijun. Electrostatic and hydrophobic interactions between ricin toxin a chain and the ribosome. Retrieved from https://doi.org/doi:10.7282/t3-q8q4-1978

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TitleElectrostatic and hydrophobic interactions between ricin toxin a chain and the ribosome
NameZhou, Yijun (author); Tumer, Nilgun E. (chair); Zheng, Steven (internal member); Hampsey, Michael (internal member); Boyd, Jeff (internal member); Dutta, Shuchismita (outside member); Rutgers University; School of Graduate Studies
Date Created2019
Other Date2019-05 (degree)
SubjectRicin -- Toxicology, Microbiology and Molecular Genetics, Ribosomes
Extent1 online resource (xiii, 114 pages) : illustrations
DescriptionRicin, a plant protein toxin produced by Ricinus communis, is one of the most potent and lethal substances known. No FDA-approved vaccine or therapeutics exist to protect against ricin intoxication. Ricin is one of the most widely studied ribosome inactivating proteins (RIPs). Interactions with the ribosome are important for the full toxicity and species specificity of ricin. Previous work in our lab showed that ricin binds to the ribosomal P-stalk to depurinate the -sarcin/ricin loop (SRL). Despite the known crystal structure of a complex between ricin toxin A chain (RTA) and a peptide corresponding to the C-termini of P proteins, little is known about how each residue at the ribosome binding site affects the depurination activity and toxicity of RTA. In chapter 1, I introduce ricin, RIPs, the ribosomal P stalk and the importance of ricin-ribosome interactions. In chapter 2, I summarize the major depurination and translation inhibition assays developed for measuring the catalytic activity of RIPs. In chapter 3, I describe how I used some of these assays to identify the important arginine residues at the stalk binding site of RTA and in chapter 4, I show that the stalk binding site also consists of a hydrophobic pocket. The effects of these arginine and hydrophobic residues on the toxicity and the enzymatic activity of RTA are discussed. The most critical arginine and hydrophobic residues are identified, and the electrostatic and hydrophobic interactions are compared. I show that toxicity of RTA can be further reduced when mutations in electrostatic and hydrophobic residues are combined. These data provide a detailed analysis of the ribosomal stalk binding site of RTA and provide evidence that it can serve as a critical target for therapeutics.
NotePh.D.
NoteIncludes bibliographical references
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/t3-q8q4-1978
LanguageEnglish
CollectionSchool of Graduate Studies Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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