抄録
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.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 20-23 |
| ページ数 | 4 |
| ジャーナル | FEBS Letters |
| 巻 | 174 |
| 発行部数 | 1 |
| DOI | |
| 出版物ステータス | 出版済み - 8 20 1984 |
| 外部発表 | Yes |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
これを引用
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8 : protein structure and Zn2+ binding. / Kohda, Daisuke; Yokoyama, Shigeyuki; Miyazawa, Tatsuo.
：: FEBS Letters, 巻 174, 番号 1, 20.08.1984, p. 20-23.研究成果: ジャーナルへの寄稿 › 記事
}
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
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.
UR - http://www.scopus.com/inward/record.url?scp=0021767557&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021767557&partnerID=8YFLogxK
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 -