A single base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation
Early biochemical data showed that aminoacyl-tRNA synthetases often displayed species-specific recognition of tRNA. We compared the ability of purified Saccharomyces cerevisiae and Escherichia coli arginyl-tRNA synthetases to aminoacylate native and transcribed yeast tRNA(Arg) as well as E. coli tRNA(Arg). The kinetic data revealed that yeast ArgRS could charge E. coli tRNA(Arg), but at a lower efficiency than it charged either the transcribed or native yeast tRNA(Arg). E. coli ArgRS can acylate only its cognate E. coli tRNA. Strikingly, a single base change from C to A at position 20 in yeast tRNA(3)(Arg) altered the species specificity. The transcript of yeast tRNA(3)(Arg)CA20 mutant was aminoacylated by E. coli ArgRS with a 10(6) increase in k(cat)/K(m) over that for aminoacylation of yeast tRNA(3)(Arg) transcript. This indicates that A20 is not only an important identity of E. coli tRNA(Arg), but is also the key to altering species-specific aminoacylation of yeast tRNA(Arg).
| Medienart: |
Artikel |
|---|
| Erscheinungsjahr: |
1999 |
|---|---|
| Erschienen: |
1999 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:1473 |
|---|---|
| Enthalten in: |
Biochimica et biophysica acta - 1473(1999), 2-3 vom: 27. Dez., Seite 356-62 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Liu, W [VerfasserIn] |
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| Themen: |
Amino Acyl-tRNA Synthetases |
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| Anmerkungen: |
Date Completed 14.02.2000 Date Revised 10.06.2019 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM105241687 |
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| 100 | 1 | |a Liu, W |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A single base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation |
| 264 | 1 | |c 1999 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 14.02.2000 | ||
| 500 | |a Date Revised 10.06.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Early biochemical data showed that aminoacyl-tRNA synthetases often displayed species-specific recognition of tRNA. We compared the ability of purified Saccharomyces cerevisiae and Escherichia coli arginyl-tRNA synthetases to aminoacylate native and transcribed yeast tRNA(Arg) as well as E. coli tRNA(Arg). The kinetic data revealed that yeast ArgRS could charge E. coli tRNA(Arg), but at a lower efficiency than it charged either the transcribed or native yeast tRNA(Arg). E. coli ArgRS can acylate only its cognate E. coli tRNA. Strikingly, a single base change from C to A at position 20 in yeast tRNA(3)(Arg) altered the species specificity. The transcript of yeast tRNA(3)(Arg)CA20 mutant was aminoacylated by E. coli ArgRS with a 10(6) increase in k(cat)/K(m) over that for aminoacylation of yeast tRNA(3)(Arg) transcript. This indicates that A20 is not only an important identity of E. coli tRNA(Arg), but is also the key to altering species-specific aminoacylation of yeast tRNA(Arg) | ||
| 650 | 4 | |a Comparative Study | |
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a RNA, Transfer, Amino Acyl |2 NLM | |
| 650 | 7 | |a Amino Acyl-tRNA Synthetases |2 NLM | |
| 650 | 7 | |a EC 6.1.1.- |2 NLM | |
| 700 | 1 | |a Huang, Y |e verfasserin |4 aut | |
| 700 | 1 | |a Eriani, G |e verfasserin |4 aut | |
| 700 | 1 | |a Gangloff, J |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, E |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Y |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochimica et biophysica acta |d 1948 |g 1473(1999), 2-3 vom: 27. Dez., Seite 356-62 |w (DE-627)NLM000000698 |x 0006-3002 |7 nnns |
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