Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain.

@article{Callaghan2003QuaternarySA,
  title={Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain.},
  author={Anastasia J. Callaghan and J. G{\"u}nter Grossmann and Yulia U Redko and Leopold L Ilag and Martin C. Moncrieffe and Martyn F. Symmons and Carol V Robinson and Kenneth J McDowall and Ben F Luisi},
  journal={Biochemistry},
  year={2003},
  volume={42 47},
  pages={13848-55}
}
RNase E is an essential endoribonuclease that plays a central role in the processing and degradation of RNA in Escherichia coli and other bacteria. Most endoribonucleases have been shown to act distributively; however, Feng et al. [(2002) Proc. Natl. Acad. Sci. U.S.A. 99, 14746-14751] have recently found that RNase E acts via a scanning mechanism. A structural explanation for the processivity of RNase E is provided here, with our finding that the conserved catalytic domain of E. coli RNase E… CONTINUE READING