Nucleic Acids Research, 1977, Vol. 4, No. 3 585-593
© 1977
Articles |
Proton magnetic resonance spectra of tRNAfMet from Thermus thermophilus


*Department of Hydrocarbon Chemistry, Faculty of Engineering, Kyoto University Kyoto 606, Japan Institute for Protein Research, Osaka University Suita, Osaka 565
Received December 7, 1976.
220 MHz proton magnetic resonance spectra of tRNAs in bulk and tRHAfMet from Thermus therwophilus have been measured and compared with those of tRNAs from E. coli. Temperature dependences and chemical shift positions of the bulk tRNAs are well explained by the difference in their GC contents. It is known that the base sequence of the double helical regions in the cloverleaf structure of T. thermophilus tRNAfMet is different from that of E. coli tRNAfMet only at two positions in T
C arm; one more C:G pair is contained instead of a U:G pair of E. coll tRNAfMet and a C:G pair of E. coli is replaced by a G:C pair. In spite of the resembrance in the base sequences, nmr patterns around 13 ppm are fairly different from each other. The difference is discussed in relation with their tertiary structures and with the origin of chemical shift displacements.
Mitsubishi-Kasei Institute of Life SciencesMinamiooya 11, Machida-shi, Tokyo 194 +Biology Division, National Cancer Center Research InstituteTsukiji, Chuo-ku, Tokyo 4, Japan