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tRNA(adenine-1-)-methyltransferase (EC 2.1.1.36) was isolated from the extreme thermophile Thermus thermophilus strain HB8. The specific activity of the enzyme is about 50 000 and the yield of activity more than 20%. The method of isolation consists of five steps and is valid for isolation of mg quantities of the enzyme. The purified protein preparation is practically homogeneous in SDS-gel electrophoresis, the position of the protein band corresponds to a molecular weight of 25 000. By gel filtration on Sephadex G-100 the molecular weight of the native protein was found to be 70 000. These data allow to suggest a subunit structure of the enzyme. The enzyme is highly thermostable and is most active at 80 degrees C. The only activity of the enzyme is to methylate A58 in the T psi X loop of tRNA.
I A Morozov, and
A S Gambarian, and
T V Venkstern
June 1994,
Bioscience, biotechnology, and biochemistry,
I A Morozov, and
A S Gambarian, and
T V Venkstern
January 2000,
Nucleic acids symposium series,
I A Morozov, and
A S Gambarian, and
T V Venkstern
October 1987,
Bioorganicheskaia khimiia,
I A Morozov, and
A S Gambarian, and
T V Venkstern
September 1993,
Nucleic acids research,
I A Morozov, and
A S Gambarian, and
T V Venkstern
January 1988,
Molekuliarnaia biologiia,
I A Morozov, and
A S Gambarian, and
T V Venkstern
August 2006,
Proteins,
I A Morozov, and
A S Gambarian, and
T V Venkstern
January 1983,
Nucleic acids symposium series,
I A Morozov, and
A S Gambarian, and
T V Venkstern
July 2006,
RNA biology,
I A Morozov, and
A S Gambarian, and
T V Venkstern
April 1987,
Bioorganicheskaia khimiia,
I A Morozov, and
A S Gambarian, and
T V Venkstern
January 1992,
Nucleic acids symposium series,
