One polypeptide with two aminoacyl-tRNA synthetase activities

Constantinos Stathopoulos; Tong Li; Randy Longman; Ute C. Vothknecht; Hubert D. Becker; Michael Ibba; Dieter Söll

doi:10.1126/science.287.5452.479

One polypeptide with two aminoacyl-tRNA synthetase activities

Constantinos Stathopoulos, Tong Li, Randy Longman, Ute C. Vothknecht, Hubert D. Becker, Michael Ibba, Dieter Söll

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

Abstract

The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.

Original language	English (US)
Pages (from-to)	479-482
Number of pages	4
Journal	Science
Volume	287
Issue number	5452
DOIs	https://doi.org/10.1126/science.287.5452.479
State	Published - Jan 21 2000
Externally published	Yes

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title = "One polypeptide with two aminoacyl-tRNA synthetase activities",

abstract = "The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.",

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T1 - One polypeptide with two aminoacyl-tRNA synthetase activities

AU - Stathopoulos, Constantinos

AU - Li, Tong

AU - Longman, Randy

AU - Vothknecht, Ute C.

AU - Becker, Hubert D.

AU - Ibba, Michael

AU - Söll, Dieter

PY - 2000/1/21

Y1 - 2000/1/21

N2 - The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.

AB - The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.

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One polypeptide with two aminoacyl-tRNA synthetase activities

Abstract

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