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Nucleic Acids Research, 2001, Vol. 29, No. 4 880-885
© 2001 Oxford University Press

Characterization of RNase P from Thermotoga maritima

Ralf Paul, Denis Lazarev1 and Sidney Altman*

Department of Molecular, Cellular and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103, USA and 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA

The protein subunit of RNase P from a thermophilic bacterium, Thermotoga maritima, was overexpressed in and purified from Escherichia coli. The cloned protein was reconstituted with the RNA subunit transcribed in vitro. The temperature optimum of the holoenzyme is near 50°C, with no enzymatic activity at 65°C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80°C. However, in heterologous reconstitution experiments in vitro with RNase P subunits from other species, we found that the protein subunit from T.maritima was responsible for the comparative thermal stability of such complexes.

* To whom correspondence should be addressed. Tel: +1 203 432 3500; Fax: +1 203 432 5713; Email: sidney.altman{at}yale.edu


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