TY - JOUR
T1 - An archaeal RNA binding protein, FAU-1, is a novel ribonuclease related to rRNA stability in Pyrococcus and Thermococcus
AU - Ikeda, Yoshiki
AU - Okada, Yasuhiro
AU - Sato, Asako
AU - Kanai, Tamotsu
AU - Tomita, Masaru
AU - Atomi, Haruyuki
AU - Kanai, Akio
N1 - Funding Information:
We thank all the members of the RNA Group and Dr. Shinnosuke Murakami at the Institute for Advanced Biosciences, Keio University, Japan, for insightful discussions and technical help. We also thank Dr. Carol Mercer and Ms. Kara Wolfe for helpful discussions and critical reading of the manuscript, Dr. Kenji Nakahigashi for valuable discussions and technical help, and Dr. Kahori Ikeda for great help in conducting this study. This research was supported, in part, by research funds from the Yamagata Prefectural Government and Tsuruoka City, Japan, and was supported, in part, by a Grant-in-Aid for Scientific Research (A) (#26242075) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
Publisher Copyright:
© 2017 The Author(s).
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85030700939&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85030700939&partnerID=8YFLogxK
U2 - 10.1038/s41598-017-13062-3
DO - 10.1038/s41598-017-13062-3
M3 - Article
C2 - 28978920
AN - SCOPUS:85030700939
SN - 2045-2322
VL - 7
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 12674
ER -