Thesis (Ph. D.)--University of Texas at Austin, 2005. / Vita. Includes bibliographical references.

Thesis (D.Sc.D.)--Boston University, Henry M. Goldman School of Graduate Dentistry, 1992 (Oral Biology). / Includes bibliographical references (leaves 70-84). / The ALG7 gene encodes the tunicamycin-sensitive, dolichol-P-dependent Nacetylglucosamine- 1-phosphate transferase, GPT, that catalyzes the synthesis of the first dolichollinked sugar, Dol-PP-GlcNAc, in the N-glycosylation pathway. ALG7 has been evQlutionarily conserved and is essential for growth in all eukaryotes. The ALG7 gene expression in yeast is known to be regulated in part by the 3' untranslated regions (UTR) of the ALG7 multiple transcripts at the posttranscriptional level. To examine the regulatory features of the mammalian ALG7 gene, cloning and characterization of the hamster ALG7 mRNAs were undertaken. Polymerase chain reaction (PCR) using a single ALG7 gene-specific primer was performed to clone the cDNAs corresponding to the 3' and 5' ends of the ALG7 mRNAs from the Chinese hamster ovary (CHO) cells. The initial Northern blot analysis using a hamster ALG7 genomic DNA as a probe has shown that in the CHO cells the ALG7 gene is transcribed into three major messages, approximately 1.5, 1.9, and 2.2 kb in size. The 1.9 kb transcripts were cloned and sequenced. There is one consensus polyadenylation signal AAUAAA located 12 nucleotides (nt) upstream to the major poly(A) site. Three additional minor poly(A) sites are located at 18, 21 and 29 nt downstream from the AAUAAA sequence in this 1.9 kb class of mRNAs. [TRUNCATED]

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A dissertation submitted to the Faculty of Science, University of the Witwatersrand, Johannesburg, in fulfilment of the requirements for the degree of Master of Science. July, 2017 / Eukaryotic protein synthesis occurs in three phases: initiation, elongation and termination. The elongation phase is mediated by elongation factors. Elongation factors are divided into elongation factor 1 (eEF1) and elongation factor 2 (eEF2). Elongation factor 1 complex are proteins that mediates the extension of growing polypeptide chains by adding one amino acid residue at a time. The eEF-1 complex comprises of four subunits, eEF1α, eEF1β, eEF1γ and eEF1δ. The β-subunit of elongation factor 1 complex (eEF1) plays a central role in the elongation step of eukaryotic protein biosynthesis, which essentially involves interaction with the α-subunits (eEF1α) and γ-subunits (eEF1γ). To biophysically characterise heEF1β, three E. coli expression vector systems was constructed for recombinant expression of the full length (FL-heEF1β), amino terminus (NT-heEF1β) and the carboxyl terminus (CT-heEF1β) regions of the protein. NT-heEF1β was created from the FL-heEF1β by site-directed mutagenesis using mutagenic forward and reverse primers. The results suggest that heEF1β is predominantly alpha-helical and possesses an accessible hydrophobic cavity in the CT-heEF1β. Both FL-heEF1β and NT-heEF1β forms dimers of size 62 kDa and 30 kDa, respectively, but the CT-heEF1β is monomeric. FL-heEF1β interacts with the N-terminus GST-like domain of heEF1γ (NT-heEF1γ) to form a 195 kDa complex, or a 230 kDa complex in the presence of oxidised glutathione. On the other hand, NT-heEF1β forms a 170 kDa complex with NT-heEF1γ and a high molecular weight aggregate of size greater than 670 kDa. This study affirms that the interaction between heEF1β and heEF1γ subunits occurs at the N-terminus regions of both proteins, also the N-terminus region of heEF1β is responsible for its dimerisation and the C-terminus region of heEF1β controls the formation of an ordered eEF1β-γ oligomer, a structure that may be essential in the elongation step of eukaryotic protein biosynthesis. / MT 2018

Thesis (Ph. D.)--University of Texas at Austin, 2001. / Vita. Includes bibliographical references. Available also from UMI Company.

Thesis (Ph. D.)--University of Texas at Austin, 2003. / Supervisors: Josef A. Käs and Tess J. Moon. Vita. Includes bibliographical references. Also available from UMI.

Thesis (Ph. D.)--University of Texas at Austin, 2002. / Vita. Includes bibliographical references. Available also from UMI Company.

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