Characterization of RNase P from Thermotoga maritima

by: Ralf Paul, Denis Lazarev, Sidney Altman

Nucl. Acids Res., Vol. 29, No. 4. (15 February 2001), pp. 880-885.

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Abstract

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 50degreesC, with no enzymatic activity at 65degreesC or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80degreesC. 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. 10.1093/nar/29.4.880

@article{citeulike:2569273, abstract = {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{degrees}C, with no enzymatic activity at 65{degrees}C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80{degrees}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. 10.1093/nar/29.4.880}, author = {Paul, Ralf and Lazarev, Denis and Altman, Sidney }, citeulike-article-id = {2569273}, doi = {10.1093/nar/29.4.880}, journal = {Nucl. Acids Res.}, keywords = {protein, rna, rnasep}, month = {February}, number = {4}, pages = {880--885}, posted-at = {2008-03-21 07:55:05}, priority = {5}, title = {Characterization of RNase P from Thermotoga maritima}, url = {http://dx.doi.org/10.1093/nar/29.4.880}, volume = {29}, year = {2001} }

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TY - JOUR ID - citeulike:2569273 L3 - citeulike-article-id:2569273 TI - Characterization of RNase P from Thermotoga maritima JF - Nucl. Acids Res. VL - 29 IS - 4 SP - 880 EP - 885 N2 - 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{degrees}C, with no enzymatic activity at 65{degrees}C or above. This finding is in sharp contrast to the optimal growth temperature of T.maritima, which is near 80{degrees}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. 10.1093/nar/29.4.880 KW - protein KW - rna KW - rnasep AU - Paul, Ralf AU - Lazarev, Denis AU - Altman, Sidney PY - 2001/02/15/ UR - http://dx.doi.org/10.1093/nar/29.4.880 ER -

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