Characterization of RNase P from Thermotoga maritima

Ralf Paul, Denis Lazarevand, Sidney Altman

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)880-885
Number of pages6
JournalNucleic acids research
Issue number4
StatePublished - Feb 15 2001
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


Dive into the research topics of 'Characterization of RNase P from Thermotoga maritima'. Together they form a unique fingerprint.

Cite this