Structural highlights
Function
RNE_ECOLI Matures 5S rRNA from its precursors from all the rRNA genes. It also cleaves RNA I, a molecule that controls the replication of colE1 plasmid DNA. It is the major endoribonuclease participating in mRNA turnover in E.coli. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process.
Publication Abstract from PubMed
The endoribonuclease RNase E is a principal factor in RNA turnover and processing that helps to exercise fine control of gene expression in bacteria. While its catalytic activity can be strongly influenced by the chemical identity of the 5' end of RNA substrates, the enzyme can also cleave numerous substrates irrespective of the chemistry of their 5' ends through a mechanism that has remained largely unexplained. We report structural and functional data illuminating details of both operational modes. Our crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage. Our data also reveal an autoinhibitory pocket that modulates the overall activity of the ribonuclease. Taking these findings together, we propose how RNase E uses versatile modes of RNA recognition to achieve optimal activity and specificity.
Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.,Bandyra KJ, Wandzik JM, Luisi BF Mol Cell. 2018 Sep 20. pii: S1097-2765(18)30699-3. doi:, 10.1016/j.molcel.2018.08.039. PMID:30270108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bandyra KJ, Wandzik JM, Luisi BF. Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E. Mol Cell. 2018 Sep 20. pii: S1097-2765(18)30699-3. doi:, 10.1016/j.molcel.2018.08.039. PMID:30270108 doi:http://dx.doi.org/10.1016/j.molcel.2018.08.039
