Lennette E T, Gorelic L, Apirion D
Proc Natl Acad Sci U S A. 1971 Dec;68(12):3140-4. doi: 10.1073/pnas.68.12.3140.
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.
大肠杆菌的一种温度敏感突变株在非允许温度下生长时,核糖核酸酶(RNase)活性显著增加。在非允许温度下生长期间,脉冲标记RNA的降解程度增加,而乳糖操纵子mRNA的功能寿命缩短。通常在大肠杆菌中稳定的T7 RNA,在该菌株的非允许温度下也保持稳定。所测定的RNase可能是细胞中mRNA正常降解机制的一部分。本文提出了一种mRNA降解机制,该机制需要内切核酸酶和3'至5'外切核酸酶的共同作用。