Abstract:
:Ribosome biogenesis and turnover are processes necessary for cell viability and proliferation, and many kinds of proteins are known to regulate these processes. However, many questions still remain, especially in the Archaea. Generally, several ribonucleases are required to process precursor rRNAs to their mature forms, and to degrade rRNAs for quality control. Here, we found that FAU-1, which is known to be an RNA binding protein, possesses an RNase activity against precursor 5S rRNA derived from P. furiosus and T. kodakarensis in the order Thermococcales in vitro. An in vitro analysis revealed that UA sequences in the upstream of 5S rRNA were preferentially degraded by addition of FAU-1. Moreover, a fau-1 gene deletion mutant of T. kodakarensis showed a delay of exponential phase, reduction of maximum cell number and significant changes in the nucleotide sequence lengths of its 5S, 16S, and 23S rRNAs in early exponential phase. Our results suggest that FAU-1 is a potential RNase involved in rRNA stability through maturation and/or degradation processes.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Ikeda Y,Okada Y,Sato A,Kanai T,Tomita M,Atomi H,Kanai Adoi
10.1038/s41598-017-13062-3subject
Has Abstractpub_date
2017-10-04 00:00:00pages
12674issue
1issn
2045-2322pii
10.1038/s41598-017-13062-3journal_volume
7pub_type
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