PMID:11134527

Citation	Liou, GG, Jane, WN, Cohen, SN, Lin, NS and Lin-Chao, S (2001) RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc. Natl. Acad. Sci. U.S.A. 98:63-8
Abstract	RNase E isolated from Escherichia coli is contained in a multicomponent "degradosome" complex with other proteins implicated in RNA decay. Earlier work has shown that the C-terminal region of RNase E is a scaffold for the binding of degradosome components and has identified specific RNase E segments necessary for its interaction with polynucleotide phosphorylase (PNPase), RhlB RNA helicase, and enolase. Here, we report electron microscopy studies that use immunogold labeling and freeze-fracture methods to show that degradosomes exist in vivo in E. coli as multicomponent structures that associate with the cytoplasmic membrane via the N-terminal region of RNase E. Whereas PNPase and enolase are present in E. coli in large excess relative to RNase E and therefore are detected in cells largely as molecules unlinked to the RNase E scaffold, immunogold labeling and biochemical analyses show that helicase is present in approximately equimolar amounts to RNase E at all cell growth stages. Our findings, which establish the existence and cellular location of RNase E-based degradosomes in vivo in E. coli, also suggest that RNA processing and decay may occur at specific sites within cells.
Links	PubMed PMC14545 Online version:10.1073/pnas.011535498
Keywords	Bacterial Proteins/metabolism; Bacterial Proteins/ultrastructure; Blotting, Western; Cell Membrane/metabolism; Cell Membrane/ultrastructure; Endoribonucleases/chemistry; Endoribonucleases/isolation & purification; Endoribonucleases/metabolism; Endoribonucleases/ultrastructure; Escherichia coli/cytology; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli/ultrastructure; Freeze Fracturing; Immunohistochemistry; Membrane Proteins/metabolism; Membrane Proteins/ultrastructure; Microscopy, Electron; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Multienzyme Complexes/ultrastructure; Polyribonucleotide Nucleotidyltransferase/isolation & purification; Polyribonucleotide Nucleotidyltransferase/metabolism; Polyribonucleotide Nucleotidyltransferase/ultrastructure; Protein Binding; RNA Helicases/isolation & purification; RNA Helicases/metabolism; RNA Helicases/ultrastructure; RNA, Bacterial/metabolism
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