Ribonucleolytic activities in the Escherichia coli in vitro translation system and in its separate components.
mRNA stability is a limiting parameter for the efficiency of in vitro protein biosynthesis. In order to develop strategies to prolong the mRNA half-life, we investigated the ribonuclease activities in the complete Escherichia coli system, in the separate cell fractions 70S ribosomes and S-100 and in the non-cellular fraction. Our results imply that the amount of ribonucleolytic activities and the insensitivity to placental RNase inhibitor in the complete system are due to the 70S ribosome fraction, whereas the generation of small degradation products is due to the S-100 fraction. Remarkably, the human placental RNase inhibitor is able to reduce mRNA degradation in the bacterial S-100 fraction.
Fuchs
U
U
Institut für Biochemie der Freien Universität Berlin, Germany.
Stiege
W
W
Erdmann
V A
VA
D002474:Cell-Free System; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism*; D006801:Humans; D010920:Placenta / Q000201:enzymology; D010926:Placental Hormones / Q000494:pharmacology; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure; D014158:Transcription, Genetic
D004791:Enzyme Inhibitors; D010926:Placental Hormones; D012333:RNA, Messenger; C022052:placental ribonuclease inhibitor; D012260:Ribonucleases