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A protein complex mediating mRNA degradation in Escherichia coli
Author(s) -
Py Béatrice,
Causton Helen,
Mudd Elisabeth A.,
Higgins Christopher F.
Publication year - 1994
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1994.tb01309.x
Subject(s) - exoribonuclease , biology , multiprotein complex , nuclease , messenger rna , rnase p , escherichia coli , degradosome , purine nucleoside phosphorylase , polynucleotide phosphorylase , biochemistry , microbiology and biotechnology , enzyme , rna , gene , purine
Summary mRNA degradation in Escherichia coli is mediated by a combination of exo‐ and endoribolucleases. We present evidence for a multiprotein complex which includes at least two enzymes that play important roles in mRNA degradation: the exoribonuclease poly‐nucleotide phosphorylase (PNPase) and the endorlbo‐nuclease RNase E. An activity which impedes the processive activity of PNPase at stem‐loop structures also appears to be associated with the complex. This complex is estimated to have a molecular mass of about 500 kDa and includes several additional poly‐peptides whose functions are unknown. The identification of a complex which includes several activities associated with mRNA degradation has implications for the mechanisms and co‐ordinated control of mRNA degradation.