TY - JOUR
T1 - Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8
T2 - protein structure and Zn2+ binding
AU - Kohda, Daisuke
AU - Yokoyama, Shigeyuki
AU - Miyazawa, Tatsuo
N1 - Funding Information:
The authorsa re gratefu1to Professor T. Oshima of Tokyo Institute of Technology for T. ther-mophilusH B8 strain and to Dr K. Fujiwara of University of Tokyo for the measurementso f atomic absorption. This work was supportedi n part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
PY - 1984/8/20
Y1 - 1984/8/20
N2 - Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases have been purified from an extreme thermophile, Thermus thermophilus HB8. Valyl-tRNA and isoleucyl-tRNA synthetases are found to be monomer proteins (Mr 108000 and 129000, respectively), while methionyl-tRNA synthetase is a dimer protein (Mr 150000). These enzymes are very similar with respect to amino acid compositions and α-helix contents as estimated by circular dichroism analyses. Furthermore, two Zn2+ are tightly bound to each of these synthetases. These data suggest that valyl-tRNA and isoleucyl-tRNA synthetases consist of two domains, each corresponding to the subunit of methionyl-tRNA synthetase.
AB - Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases have been purified from an extreme thermophile, Thermus thermophilus HB8. Valyl-tRNA and isoleucyl-tRNA synthetases are found to be monomer proteins (Mr 108000 and 129000, respectively), while methionyl-tRNA synthetase is a dimer protein (Mr 150000). These enzymes are very similar with respect to amino acid compositions and α-helix contents as estimated by circular dichroism analyses. Furthermore, two Zn2+ are tightly bound to each of these synthetases. These data suggest that valyl-tRNA and isoleucyl-tRNA synthetases consist of two domains, each corresponding to the subunit of methionyl-tRNA synthetase.
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U2 - 10.1016/0014-5793(84)81069-8
DO - 10.1016/0014-5793(84)81069-8
M3 - Article
C2 - 6468656
AN - SCOPUS:0021767557
VL - 174
SP - 20
EP - 23
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1
ER -