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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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The universally conserved NTPase OLA1
Jessica Semmelrock1, Hans-Joachim Wieden2
1Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, AB, Canada.
Abstract:
The non-canonical translation factor OBG-like ATPase 1 (OLA1) is conserved across all domains of life. OLA1 has been studied for decades by many groups, often under different names such as GBP45, GTBP9, DOC45, PTD004, EngD, YyaF, Ybr025c, and in bacteria, YchF. Studies have correlated OLA1 with iron metabolism, oxidative stress response, mediation of temperature stress, and virulence. OLA1 has gained attention for its implicated role in a wide range of health conditions and cellular processes including cancer, centrosome regulation/cell proliferation, heart disease, persistent pulmonary hypertension of the newborn, mitochondrial function, neuronal differentiation, protein degradation, atherosclerosis, Down's syndrome, as well as ribosome-dependent protein synthesis. On the background of such a wide range of functional implications, insight into the molecular mechanism of the evolutionarily ancient OLA1 will help to explain the breadth of phenotypic traits. Information about the different protein structural domains present in OLA1 and results from OLA1 in vivo and in vitro studies suggest a role in ribosome-dependent translation regulation based on molecular mimicry with the canonical translation factors.
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