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Full-Text Articles in Life Sciences
Global And Specific Controls Of Protein Synthesis In Hibernators, Peipei Pan
Global And Specific Controls Of Protein Synthesis In Hibernators, Peipei Pan
UNLV Theses, Dissertations, Professional Papers, and Capstones
Mammalian hibernation is a highly dynamic physiological process that is composed of a series of torpor bouts, wherein hibernators oscillate between periods of torpor and interbout arousal. Although normally vital to homeostasis, many energetically consumptive processes such as translation or protein synthesis are virtually ceased during hibernation. Earlier studies indicated that protein synthesis had fallen to almost negligible levels. Cap-dependent initiation of translation is well regulated by eukaryotic translation initiation factor 4E (eIF4E) and its binding partner eIF4E-binding protein 1 (4E-BP1) when hibernators cycle in and out the torpor state. Herein, I investigated well-characterized regulatory mechanisms of global and specific …
The Mitospecific Region Of Mrp20 And Its Importance For The Assembly Of Mitochondrial Ribosomes In Saccharomyces Cerevisiae, Jasvinder Kaur
The Mitospecific Region Of Mrp20 And Its Importance For The Assembly Of Mitochondrial Ribosomes In Saccharomyces Cerevisiae, Jasvinder Kaur
Dissertations (1934 -)
Yeast mitochondrial ribosomes are composed of an rRNA scaffold, encoded by the mitochondrial genome and many different proteins, which, with the exception of one, are encoded by nuclear genes. These ribosomal proteins are imported into the mitochondrial matrix following their synthesis in the cytosol, however, little is known about the subsequent events which result in an assembled, translationally-competent ribosome. Many of the mitochondrial ribosomal proteins bear homology to bacterial ancestors. In addition to the acquisition of mitochondrial targeting signals, a number of these nuclearly-encoded ribosomal proteins have acquired additional domains, often at their C-termini, which are termed "mitochondrial-specific domains". The …