The sequence of sites recognised by a member of the RNase E/G family can control the maximal rate of cleavage, while a 5'-monophosphorylated end appears to function cooperatively in mediating RNA binding.

Biochemical and Biophysical Research Communications
Stefanie S JourdanKenneth J McDowall

Abstract

Members of the RNase E/G family are multimeric, 5'-end-sensing, single-strand-specific endoribonucleases that are found in chloroplasts as well as bacteria, and have central roles in RNA processing and degradation. A well-studied member of this family is Escherichia coli RNase G. Recently, we have shown that the interaction of this enzyme with a 5'-monophosphorylated end can enhance substrate binding in vitro and the decay of mRNA in vivo. We show here that a single-stranded site despite not being sufficient for rapid cleavage makes a substantial contribution to the binding of RNase G. Moreover, we find that the sequence of a site bound by RNase G can moderate the maximal rate by at least an order of magnitude. This supports a model for the RNase E/G family in which a single-stranded segment(s) can cooperate in the binding of enzyme that subsequently cleaves preferentially at another site. We also provide evidence that in order to promote cleavage a 5'-monophosphorylated end needs to be linked physically to a single-stranded site, indicating that it functions cooperatively. Our results are discussed in terms of recent X-ray crystal structures and models for the initiation of bacterial mRNA degradation.

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Citations

Mar 1, 2012·Journal of Industrial Microbiology & Biotechnology·Ryan ManowShengde Zhou
Jan 24, 2014·Nucleic Acids Research·Louise KimeKenneth J McDowall
Sep 23, 2014·Nucleic Acids Research·Justin E ClarkeKenneth J McDowall
Aug 26, 2015·Proceedings of the National Academy of Sciences of the United States of America·Mona W OrrVincent T Lee
Mar 19, 2013·Biochimica Et Biophysica Acta·David LalaounaEric Massé
Jan 16, 2021·Genes & Development·Christopher J MooreKangseok Lee

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