Open Access. Powered by Scholars. Published by Universities.®
- Discipline
Articles 1 - 3 of 3
Full-Text Articles in Molecular Biology
Protein Degradation Regulates Phospholipid Biosynthetic Gene Expression In Saccharomyces Cerevisiae, Bryan Salas-Santiago
Protein Degradation Regulates Phospholipid Biosynthetic Gene Expression In Saccharomyces Cerevisiae, Bryan Salas-Santiago
Doctoral Dissertations
Transcriptional regulation of most phospholipid biosynthetic genes in Saccharomyces cerevisiae is coordinated by inositol and choline. Inositol affects phosphatidic acid (PA) intracellular levels. Opi1p interacts physically with PA and is the main repressor of the phospholipid biosynthetic genes. It is localized in the endoplasmic reticulum (ER) bound to the ER membrane protein Scs2p. When PA levels drop, Opi1p is translocated into the nucleus repressing most phospholipid biosynthetic genes. The OPI1 locus was identified in a screen looking for overproduction and excretion of inositol (Opi-). Opi- mutants are generally associated with a defect in …
Identifying Functional Components Of The Endoplasmic Reticulum Quality Control And Degradation Factor Edem1, Lydia Lamriben
Identifying Functional Components Of The Endoplasmic Reticulum Quality Control And Degradation Factor Edem1, Lydia Lamriben
Doctoral Dissertations
The ER Degradation-Enhancing Mannosidase-Like protein 1 (EDEM1) is a critical endoplasmic reticulum (ER) quality control factor involved in identifying and directing non-native proteins to the ER-associated protein degradation (ERAD) pathway. However, its recognition and binding properties have remained enigmatic since its discovery. Here we provide evidence for an additional redox-sensitive interaction between EDEM1 and Z/NHK that requires the presence of the single Cys on the α-1 antitrypsin ERAD clients. Moreover, this Cys-dependent interaction is necessary when the proteins are isolated under stringent detergent conditions, ones in which only strong covalent interactions can be sustained. This interaction is inherent to the …
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 …