Cellular roles of the human Obg-like ATPase 1 (hOLA1) and its YchF homologs
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Date
2020
Authors
Balasingam, Nirujah
Brandon, Harland E.
Ross, Joseph A.
Wieden, Hans-Joachim
Thakor, Nehal
Journal Title
Journal ISSN
Volume Title
Publisher
Canadian Science Publishing
Abstract
P-loop NTPases comprise one of the major superfamilies of nucleotide binding proteins, which mediate a variety of cellular processes, such as mRNA translation, signal transduction, cell motility, and growth regulation. In this review, we discuss the structure and function of two members of the ancient Obg-related family of P-loop GTPases: human Obg-like ATPase 1 (hOLA1), and its bacterial/plant homolog, YchF. After a brief discussion of nucleotide binding proteins in general and the classification of the Obg-related family in particular, we discuss the sequence and structural features of YchF and hOLA1. We then explore the various functional roles of hOLA1 in mammalian cells during stress response and cancer progression, and of YchF in bacterial cells. Finally, we directly compare and contrast the structure and function of hOLA1 with YchF before summarizing the future perspectives of hOLA1 research. This review is timely, given the variety of recent studies aimed at understanding the roles of hOLA1 and YchF in such critical processes as cellular-stress response, oncogenesis, and protein synthesis.
Description
Permission to archive accepted author manuscript.
Keywords
hOLA1 , YchF , Cellular stress , Cancer progression , Structure-function
Citation
Balasingam, N., Brandon, H. E., Ross, J. A., Wieden, H.-J., & Thakor, N. (2020). Cellular roles of human Obg-like ATPase 1 (hOLA1) and its YchF homologs. Biochemistry and Cell Biology, 98(1), 1-11. doi: 10.1139/bcb-2018-0353