Open AccessA new role for RNase II in mRNA decay: Striking differences between RNase II mutants and similarities with a strain deficient in RNase E
Author(s) -
Cruz Ana Alexandra,
Marujo Paulo Emanuel,
Newbury Sarah Faith,
Arraiano Cecilia Maria
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08595.x
Subject(s) - polynucleotide phosphorylase , endoribonuclease , ribonuclease , rnase p , ribonuclease iii , rnase mrp , mutant , microbiology and biotechnology , messenger rna , biology , rnase ph , escherichia coli , biochemistry , enzyme , rnase h , rna , cold shock domain , chemistry , gene , purine nucleoside phosphorylase , purine , rna interference
The effect of Escherichia coli ribonuclease II and polynucleotide phosphorylase was analysed on the degradation of Desulfovibrio vulgaris cytochrome c 3 ( cyc ) mRNA. In the absence of these exoribonucleolytic activities, cyc mRNA was stabilised but the two enzymes had a different role in its decay. Surprisingly, a temperature‐sensitive mutation in ribonuclease II gave a degradation pattern similar to what had been observed in the absence of endoribonuclease E activity. In an RNase II deletion mutant this was not observed. We propose and verify a model in which the temperature‐sensitive ribonuclease II interferes with the action of ribonuclease E.