Characterization of RNase P from Thermotoga maritima | Zendy

Rajani Kr. Paul | Zendy

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Characterization of RNase P from Thermotoga maritima

Author(s) -

Rajani Kr. Paul

Publication year - 2001

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/29.4.880

Subject(s) - thermotoga maritima , biology , escherichia coli , rnase p , protein subunit , thermophile , heterologous , rnase h , biochemistry , rna , enzyme , microbiology and biotechnology , gene

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.

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