Date of Completion

3-3-2020

Embargo Period

8-29-2020

Keywords

BipA, E. coli, Adaptation, Physiology

Major Advisor

Dr. David Benson

Co-Major Advisor

Dr. Victoria Robinson

Associate Advisor

Dr. Daniel Gage

Associate Advisor

Dr. Joerg Graf

Associate Advisor

Dr. Kenneth Campellone

Field of Study

Molecular and Cell Biology

Degree

Doctor of Philosophy

Open Access

Open Access

Abstract

BipA, also known as TypA, is a highly conserved protein originally identified in Salmonella typhimurium as a protein that is induced in response to bactericidal/permeability-inducing protein. Mutants lacking BipA exhibit a wide variety of phenotypes. Some of these phenotypes include: diminished pathogenicity, altered capsule biosynthesis, decreased resistance to antibiotics and antimicrobial peptides, as well as diminished growth at low temperatures. These data suggest that BipA affects multiple systems throughout the cell, suggesting that BipA plays a role in adaptation to various conditions within the cell. A similar role has been proposed for RelA although effecting transcription during adaptation rather than translation. I propose here that BipA is involved in the stringent response at the level of translation and may interact with RelA when conditions in the cell change.

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