Abstract
The tRNA modifying enzyme, S-adenosylmethionine:tRNA(guanine-7-)-methyltransferase, has been extensively purified from Salmonella typhimurium. A rapid and efficient purification method using phosphocellulose chromatography followed by ammonium sulfate precipitation and Sephadex G-100 gel filtration is described. The enzyme appears to be a single polypeptide chain with a molecular weight of approximately 25 000-30 000 daltons. The Km for S-adenosylmethionine and for undermethylated tRNA is 53 μ M and 3.4 μM, respectively. The methylation reaction is dependent on added monovalent or divalent cations; 5 mM spermidine, 3 mM MgCl2 and 1 mM spermine are the most effective. The enzyme, though not homogeneous, is free from contaminating ribonucleases and other tRNA methyltransferases.
| Original language | English |
|---|---|
| Pages (from-to) | 97-106 |
| Number of pages | 10 |
| Journal | Molecular and Cellular Biochemistry |
| Volume | 52 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Sep 1983 |
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ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Clinical Biochemistry
- Cell Biology
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Isolation and characterization of a tRNA(guanine-7-)-methyltransferase from Salmonella typhimurium. / Colonna, Alfredo; Ciliberto, Gennaro; Santamaria, Rita; Cimino, Filiberto; Salvatore, Francesco.
In: Molecular and Cellular Biochemistry, Vol. 52, No. 2, 09.1983, p. 97-106.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Isolation and characterization of a tRNA(guanine-7-)-methyltransferase from Salmonella typhimurium
AU - Colonna, Alfredo
AU - Ciliberto, Gennaro
AU - Santamaria, Rita
AU - Cimino, Filiberto
AU - Salvatore, Francesco
PY - 1983/9
Y1 - 1983/9
N2 - The tRNA modifying enzyme, S-adenosylmethionine:tRNA(guanine-7-)-methyltransferase, has been extensively purified from Salmonella typhimurium. A rapid and efficient purification method using phosphocellulose chromatography followed by ammonium sulfate precipitation and Sephadex G-100 gel filtration is described. The enzyme appears to be a single polypeptide chain with a molecular weight of approximately 25 000-30 000 daltons. The Km for S-adenosylmethionine and for undermethylated tRNA is 53 μ M and 3.4 μM, respectively. The methylation reaction is dependent on added monovalent or divalent cations; 5 mM spermidine, 3 mM MgCl2 and 1 mM spermine are the most effective. The enzyme, though not homogeneous, is free from contaminating ribonucleases and other tRNA methyltransferases.
AB - The tRNA modifying enzyme, S-adenosylmethionine:tRNA(guanine-7-)-methyltransferase, has been extensively purified from Salmonella typhimurium. A rapid and efficient purification method using phosphocellulose chromatography followed by ammonium sulfate precipitation and Sephadex G-100 gel filtration is described. The enzyme appears to be a single polypeptide chain with a molecular weight of approximately 25 000-30 000 daltons. The Km for S-adenosylmethionine and for undermethylated tRNA is 53 μ M and 3.4 μM, respectively. The methylation reaction is dependent on added monovalent or divalent cations; 5 mM spermidine, 3 mM MgCl2 and 1 mM spermine are the most effective. The enzyme, though not homogeneous, is free from contaminating ribonucleases and other tRNA methyltransferases.
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U2 - 10.1007/BF00224919
DO - 10.1007/BF00224919
M3 - Article
C2 - 6348510
AN - SCOPUS:0020668796
VL - 52
SP - 97
EP - 106
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
SN - 0300-8177
IS - 2
ER -