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 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 evolutionary ancient OLA1 will help to explain the breadth of phenotypic traits. Information about the different protein structural domains present in OLA1 and results fromOLA1 in vivo and in vitro studies suggest a role in ribosome dependent translation regulation based on molecular mimicry with the canonical translation factors.
Semmelrock et al. (Thu,) studied this question.
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