Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 484, Issue 3, Pages 612-617Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.01.149
Keywords
YBEY; C21orf57; RNase; Yeast
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Funding
- National Institutes of Health [GM31010, GM17151]
- Welch Foundation [F-1870]
- U.S. Army Research Office [W911NF-16-1-0146]
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The product of the human C21orfS7 (huYBEY) gene is predicted to be a homologue of the highly conserved YbeY proteins found in nearly all bacteria. We show that, like its bacterial and chloroplast counterparts, the HuYbeY protein is an RNase and that it retains sufficient function in common with bacterial YbeY proteins to partially suppress numerous aspects of the complex phenotype of an Escherichia coli Delta ybeY mutant. Expression of HuYbeY in Saccharomyces cerevisiae, which lacks a YbeY homologue, results in a severe growth phenotype. This observation suggests that the function of HuYbeY in human cells is likely regulated through specific interactions with partner proteins similarly to the way YbeY is regulated in bacteria. (C) 2017 Elsevier Inc. All rights reserved.
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