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Articles 1 - 2 of 2
Full-Text Articles in Microbial Physiology
Gata-Family Transcription Factors In Magnaporthe Oryzae, Cristian F. Quispe
Gata-Family Transcription Factors In Magnaporthe Oryzae, Cristian F. Quispe
Department of Agronomy and Horticulture: Dissertations, Theses, and Student Research
The filamentous fungus, Magnaporthe oryzae, responsible for blast rice disease, destroys around 10-30% of the rice crop annually. Infection begins when the specialized infection structure, the appressorium, generates enormous internal turgor pressure through the accumulation of glycerol. This turgor acts on a penetration peg emerging at the base of the cell, causing it to breach the leaf surface allowing its infection.
The enzyme trehalose-6- phosphate synthase (Tps1) is a central regulator of the transition from appressorium development to infectious hyphal growth. In the first chapter we show that initiation of rice blast disease requires a regulatory mechanism involving an …
Requirement Of Ssdelseed-Motif Of Escherichia Coli F1FO Atp Synthase In Antimicrobial Peptide Binding., Junior Kom Tayou
Requirement Of Ssdelseed-Motif Of Escherichia Coli F1FO Atp Synthase In Antimicrobial Peptide Binding., Junior Kom Tayou
Electronic Theses and Dissertations
F1FO ATP synthase is a membrane bound enzyme capable of synthesizing and hydrolyzing ATP. Lately, α-helical cationic peptides such as melittin and melittin related peptide (MRP) were shown to inhibit E. coli ATP synthase. The proposed but unconfirmed site of inhibition is βDELSEED-motif formed by the residues 380-386, located at the interface of α/β subunit of ATP synthase. This project was a mutagenic analysis of βDELSEED-motif residues to understand the binding mechanism and mode of action of peptide inhibitors. The study addressed 2 main questions: Are the antibacterial/anticancer effects of these peptides related to their inhibitory action …