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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Expression, Localization, And Kinetic Characterization Of The Phospholipid Biosynthesis Enzyme Ctp: Phosphocholine Cytidylyltransferase From The Protozoan Parasite Leishmania Major, Justin Daniel Theodore Lange
Expression, Localization, And Kinetic Characterization Of The Phospholipid Biosynthesis Enzyme Ctp: Phosphocholine Cytidylyltransferase From The Protozoan Parasite Leishmania Major, Justin Daniel Theodore Lange
Theses and Dissertations
The eukaryotic parasite Leishmania is the causative agent of the disease leishmaniasis. L. major is the most common of 21 species that causes visceral leishmaniasis in humans, and 30 that cause the same disease in other mammals. Visceral leishmaniasis causes fever, weight loss, and over a short amount of time, multiple organ failure, and has a 100% mortality rate within 2 years. This makes it the second largest parasitic killer in the world behind malaria. Over 90% of the worldâ??s cases of visceral leishmaniasis have been reported in underdeveloped countries of India, Bangladesh, Nepal, Sudan, Ethiopia and Brazil, with 500,000 …
Role Of Molecular Chaperones In G Protein B5-Regulator Of G Protein Signaling Dimer Assembly And G Protein By Dimer Specificity, Alyson Cerny Howlett
Role Of Molecular Chaperones In G Protein B5-Regulator Of G Protein Signaling Dimer Assembly And G Protein By Dimer Specificity, Alyson Cerny Howlett
Theses and Dissertations
In order for G protein signaling to occur, the G protein heterotrimer must be assembled from its nascent polypeptides. The most difficult step in this process is the formation of the Gβγ dimer from the free subunits since both are unstable in the absence of the other. Recent studies have shown that phosducin-like protein (PhLP1) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold Gβ and mediate its interaction with Gγ. However, these studies did not address questions concerning the scope of PhLP1 and CCT-mediated Gβγ assembly, which are important questions given that there are four Gβs …
The Role Of Phosducin-Like Protein As A Co-Chaperone With The Cytosolic Chaperonin Complex In Assembly Of The G Protein Βγ Subunit Dimer, Paul Jayson Ludtke
The Role Of Phosducin-Like Protein As A Co-Chaperone With The Cytosolic Chaperonin Complex In Assembly Of The G Protein Βγ Subunit Dimer, Paul Jayson Ludtke
Theses and Dissertations
Phosducin-like protein (PhLP) has been shown to interact with the cytosolic chaperonin containing TCP-1 (CCT), and the βγ subunit dimer of heterotrimeric G proteins (Gβγ). Here we provide details obtained from cryo-electron microscopic and biochemical studies on the structure of the complex between the cytosolic chaperonin CCT and PhLP. Binding of PhLP to CCT occurs through only one of the two chaperonin rings, making multiple contacts with CCT through both its N- and C-terminal domains. In addition, we show that PhLP acts as a co-chaperonin along with CCT in mediating the assembly of the G protein βγ subunit and that …
The Mechanism Of Assembly Of The G-Protein Beta Gamma Subunit Dimer By Ck2 Phosphorylated Phosducin-Like Protein And The Chaperonin Containing Tcp-1, Christine M. Baker
The Mechanism Of Assembly Of The G-Protein Beta Gamma Subunit Dimer By Ck2 Phosphorylated Phosducin-Like Protein And The Chaperonin Containing Tcp-1, Christine M. Baker
Theses and Dissertations
Phosducin-like protein (PhLP) binds G-protein beta gamma subunits and is thought to assist in assembly of the G-protein beta gamma dimer. Phosphorylation of PhLP at serine residues 18-20 by the casein kinase 2 (CK2) appears to play an essential role in this process. PhLP has also been shown to interact with the chaperonin containing TCP-1 (CCT) atop its apical domain, not entering the substrate folding cavity. However, the physiological role of the PhLP-CCT interaction in G-protein beta gamma dimer formation remains unclear. This study addresses the mechanism of G-protein beta gamma assembly by exploring the specific roles of CCT and …