An archaeal RNA binding protein, FAU-1, is a novel ribonuclease related to rRNA stability in Pyrococcus and Thermococcus
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-13062-3.pdf
Reference52 articles.
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2. Finn, R. D. et al. Pfam: the protein families database. Nucleic Acids Res. 42, D222–230, https://doi.org/10.1093/nar/gkt1223 (2014).
3. Callaghan, A. J. et al. Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover. Nature 437, 1187–1191, https://doi.org/10.1038/nature04084 (2005).
4. Garrey, S. M. & Mackie, G. A. Roles of the 5′-phosphate sensor domain in RNase E. Mol. Microbiol. 80, 1613–1624, https://doi.org/10.1111/j.1365-2958.2011.07670.x (2011).
5. Henras, A. K. et al. The post-transcriptional steps of eukaryotic ribosome biogenesis. Cell. Mol. Life Sci. 65, 2334–2359, https://doi.org/10.1007/s00018-008-8027-0 (2008).
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1. Homo-trimeric structure of the ribonuclease for rRNA processing, FAU-1, from Pyrococcus furiosus;The Journal of Biochemistry;2024-02-01
2. The 23S Ribosomal RNA From Pyrococcus furiosus Is Circularly Permuted;Frontiers in Microbiology;2020-12-10
3. Insights into RNA-processing pathways and associated RNA-degrading enzymes in Archaea;FEMS Microbiology Reviews;2018-04-19
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