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Reconstitution and analysis of the multienzyme Escherichia coli RNA degradosome.
- Source :
-
Journal of molecular biology [J Mol Biol] 2008 Oct 17; Vol. 382 (4), pp. 870-83. Date of Electronic Publication: 2008 Jul 27. - Publication Year :
- 2008
-
Abstract
- The Escherichia coli RNA degradosome is a multienzyme assembly that functions in transcript turnover and maturation of structured RNA precursors. We have developed a procedure to reconstitute the RNA degradosome from recombinant components using modular coexpression vectors. The reconstituted assembly can be purified on a scale that has enabled biochemical and biophysical analyses, and we compare the properties of recombinant and cell-extracted RNA degradosomes. We present evidence that auxiliary protein components can be recruited to the 'superprotomer' core of the assembly through a dynamic equilibrium involving RNA intermediaries. We discuss the implications for the regulation of RNA degradosome function in vivo.
- Subjects :
- DEAD-box RNA Helicases chemistry
DEAD-box RNA Helicases genetics
Escherichia coli genetics
Escherichia coli Proteins genetics
Genetic Vectors genetics
Genetic Vectors metabolism
Host Factor 1 Protein chemistry
Host Factor 1 Protein genetics
Host Factor 1 Protein metabolism
Nucleic Acid Conformation
Phosphopyruvate Hydratase chemistry
Phosphopyruvate Hydratase genetics
RNA Precursors genetics
RNA Precursors metabolism
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Endoribonucleases chemistry
Endoribonucleases genetics
Endoribonucleases metabolism
Escherichia coli enzymology
Escherichia coli Proteins chemistry
Escherichia coli Proteins metabolism
Multienzyme Complexes chemistry
Multienzyme Complexes metabolism
Polyribonucleotide Nucleotidyltransferase chemistry
Polyribonucleotide Nucleotidyltransferase genetics
Polyribonucleotide Nucleotidyltransferase metabolism
RNA Helicases chemistry
RNA Helicases metabolism
RNA, Bacterial metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1089-8638
- Volume :
- 382
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 18691600
- Full Text :
- https://doi.org/10.1016/j.jmb.2008.07.059