期刊
MOLECULAR MICROBIOLOGY
卷 106, 期 3, 页码 351-366出版社
WILEY
DOI: 10.1111/mmi.13769
关键词
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资金
- National Natural Science Foundation of China [31430001, 31670049, 31100035, 31270792]
- Youth Innovation Promotion Association CAS
RNase J, a prokaryotic 5-3 exo/endoribonuclease, contributes to mRNA decay, rRNA maturation and post-transcriptional regulation. Yet the processive-exoribonucleolysis mechanism remains obscure. Here, we solved the first RNA-free and RNA-bound structures of an archaeal RNase J, and through intensive biochemical studies provided detailed mechanistic insights into the catalysis and processivity. Distinct dimerization/tetramerization patterns were observed for archaeal and bacterial RNase Js, and unique archaeal Loops I and II were found involved in RNA interaction. A hydrogen-bond-network was identified for the first time that assists catalysis by facilitating efficient proton transfer in the catalytic center. A conserved 5-monophosphate-binding pocket that coordinates the RNA 5-end ensures the 5-monophosphate preferential exoribonucleolysis. To achieve exoribonucleolytic processivity, the 5-monophosphate-binding pocket and nucleotide +4 binding site anchor RNA within the catalytic track; the 5-capping residue Leu37 of the sandwich pocket coupled with the 5-monophosphate-binding pocket are dedicated to translocating and controlling the RNA orientation for each exoribonucleolytic cycle. The processive-exoribonucleolysis mechanism was verified as conserved in bacterial RNase J and also exposes striking parallels with the non-homologous eukaryotic 5-3 exoribonuclease, Xrn1. The findings in this work shed light on not only the molecular mechanism of the RNase J family, but also the evolutionary convergence of divergent exoribonucleases.
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