Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis

ABSTRACT: Biogenesis of the essential precursor of the bacterial cell envelope, glucosamine-6-phosphate (GlcN6P), is controlled by intricate post-transcriptional networks mediated by GlmZ, a small regulatory RNA (sRNA). GlmZ stimulates translation of the mRNA encoding GlcN6P synthetase in Escherichia coli, but when bound by RapZ protein, the sRNA becomes inactivated through endoribonuclease RNase E-mediated cleavage. Here we report the cryoEM structure of the RapZ:GlmZ complex, revealing a complementary match of the RapZ tetrameric quaternary structure to structural repeats in the sRNA. The nucleic acid is contacted mostly through a highly conserved RapZ domain that shares an evolutionary relationship with phosphofructokinase and suggests links between metabolism and riboregulation. We also present

SUBMITTER: Dr. Md., Saiful Islam 

PROVIDER: S-SCDT-10_15252-EMBJ_2022112574 | biostudies-other |

REPOSITORIES: biostudies-other