Ribonuclease PH interacts with an acidic ribonuclease E site through a basic 80-amino acid domain.
In this work, we characterize the domains for the in vivo interaction between ribonuclease E (RNase E) and ribonuclease PH (RNase PH). We initially explored the interaction using pull-down assays with full wild-type proteins expressed from a chromosomal monocopy gene. Once the interaction was confirmed, we narrowed down the sites of interaction in each enzyme to an acidic 16-amino acid region in the carboxy-terminal domain of RNase E and a basic 80-amino acid region in RNase PH including an α3 helix. Our results suggest two novel functional domains of interaction between ribonucleases.
Departamento de Genética y Biología Molecular, Centro de Investigación y Estudios Avanzados del IPN, Mexico DF, Mexico.
Víctor Pérez-Medina
VP
Martínez
Gianni
G
Dehò
Robert W
RW
Simons
Jaime
J
García-Mena
D000596:Amino Acids / Q000378:metabolism*; D002498:Centrifugation; D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D005095:Exoribonucleases / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping
D000596:Amino Acids; C056502:ribonuclease PH; D004722:Endoribonucleases; D005095:Exoribonucleases; C022537:ribonuclease E
RNase E; RNase PH; domain of interaction; protein interaction