Functional relationship between Escherichia coli RNase E and the CafA protein.
We analyzed the functional relationship between the Escherichia coli RNase E and the CafA protein, which show extensive sequence similarity. The temperature-sensitive growth of the RNase E mutant strain ams1 was partially suppressed by multicopy plasmids bearing the cafA gene. Introduction of a cafA::cat mutation enhanced the temperature sensitivity of the ams1 mutant. These results suggest that there is a functional homology between these two proteins.
Wachi
M
M
Department of Bioengineering, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.
Umitsuki
G
G
Nagai
K
K
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D016254:Mutagenesis, Insertional; D013696:Temperature
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D004722:Endoribonucleases; C081905:rng protein, E coli; C022537:ribonuclease E