An Escherichia coli Mutant with Increased Messenger Ribonuclease Activity
AUTOR(ES)
Lennette, Evelyne T.
RESUMO
A temperature-sensitive mutant strain of Escherichia coli exhibits a remarkable increase in RNase activity when grown at its nonpermissive temperature. During growth at the nonpermissive temperature, there is an increase in the extent of breakdown of pulse-labeled RNA and a decrease in the functional lifetime of the mRNA for the lac operon. T7 RNA, which is usually stable in E. coli, is also stable in this strain at the nonpermissive temperature. It is possible that the RNase measured is part of the normal mechanism of mRNA degradation in the cell. A mechanism for mRNA degradation that requires the combined action of endonuclease(s) and 3′ to 5′ exonuclease(s) is proposed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389608Documentos Relacionados
- Increased stability of polysomes in an Escherichia coli mutant with relaxed control of RNA synthesis.
- An Escherichia coli Mutant with an Altered Elongation Factor Tu
- Assimilatory sulfate reduction in an Escherichia coli mutant lacking thioredoxin activity.
- Characterization of an Escherichia coli Mutant Deficient in Dihydrolipoyl Dehydrogenase Activity
- Ribonuclease II Activity in a “Presumptive” Ribonuclease II-Deficient Mutant