Substrate-dependent effects of quaternary structure on RNase E activity.

RNase E is an essential, multifunctional ribonuclease encoded in E. coli by the rne gene. Structural analysis indicates that the ribonucleolytic activity of this enzyme is conferred by rne-encoded polypeptide chains that (1) dimerize to form a catalytic site at the protein-protein interface, and (2) multimerize further to generate a tetrameric quaternary structure consisting of two dimerized Rne-peptide chains. We identify here a mutation in the Rne protein's catalytic region (E429G), as well as a bacterial cell wall peptidoglycan hydrolase (Amidase C [AmiC]), that selectively affect the specific activity of the RNase E enzyme on long RNA substrates, but not on short synthetic oligonucleotides, by enhancing enzyme multimerization. Unlike the increase in specific activity that accompanies concentration-induced multimerization, enhanced multimerization associated with either the E429G mutation or interaction of the Rne protein with AmiC is independent of the substrate's 5' terminus phosphorylation state. Our findings reveal a previously unsuspected substrate length-dependent regulatory role for RNase E quaternary structure and identify cis-acting and trans-acting factors that mediate such regulation. © 2021 Moore et al.; Published by Cold Spring Harbor Laboratory Press.

Citation

Christopher J Moore, Hayoung Go, Eunkyoung Shin, Hye-Jeong Ha, Saemee Song, Nam-Chul Ha, Yong-Hak Kim, Stanley N Cohen, Kangseok Lee. Substrate-dependent effects of quaternary structure on RNase E activity. Genes & development. 2021 Feb 01;35(3-4):286-299

Mesh Tags

Substances

PMID: 33446571

search → result