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Full-Text Articles in Biochemistry
Caulobacter Clpxp Adaptor Popa’S Domain Interactions In The Adaptor Hierarchy Of Ctra Degradation, Thomas P. Scudder
Caulobacter Clpxp Adaptor Popa’S Domain Interactions In The Adaptor Hierarchy Of Ctra Degradation, Thomas P. Scudder
Masters Theses
The degradation and recycling of protein is a process essential for the maintenance and regulation of cellular function. More specifically, in Caulobacter crescentus, the ClpXP protease is responsible for driving progression through the cell cycle and protein quality control. This protease utilizes three known adaptors to selectively degrade proteins that initiate different stages of development. This thesis will elaborate on the specific binding interface on one of these adaptors, PopA, with another, RcdA, and focus in on specific residues on PopA and investigate their roles in adaptor binding and delivery of CtrA, the master regulator of Caulobacter. Finally, I …
Adaptors At Work: Regulation Of Bacterial Proteolysis By Adaptor Hierarchies, Kamal Joshi
Adaptors At Work: Regulation Of Bacterial Proteolysis By Adaptor Hierarchies, Kamal Joshi
Doctoral Dissertations
Regulated protein degradation is essential for all life. Bacteria use energy-dependent proteases to regulate protein degradation. Recognition of a substrate is enabled by the inherent specificity of the protease and by the use of adaptor proteins that widen the spectrum of recognized substrates. In Caulobacter crescentus, the timed destruction of many regulators including CtrA by the ClpXP protease drives cell cycle progression. Although, in a test tube, ClpXP can degrade CtrA by itself and does not need any helping factors, additional factors such as CpdR, RcdA and PopA are required in vivo. Understanding how these factors modulate protease …
Control Of Proteolysis During The Caulobacter Cell Cycle, Joanne Lau
Control Of Proteolysis During The Caulobacter Cell Cycle, Joanne Lau
Doctoral Dissertations
Intracellular protein destruction is a carefully coordinated and timed regulatory mechanism that cells utilize to modulate growth, adaptation to environmental cues, and survival. In Caulobacter crescentus, a bacterium known for studies of bacterial cell division cycle, the response regulator CpdR couples phosphorylation events with the AAA+ protease ClpXP to provide punctuated degradation of crucial substrates involved in cell cycle regulation. CpdR functions like an adaptor to alter substrate choice by ClpXP, however it remains unclear how CpdR influences its multiple targets. In this thesis, we show that, unlike canonical ClpXP adaptors, CpdR alone does not strongly bind its substrate. …