Glutaminyl-tRNA synthetase: From genetics to molecular recognition

Michael Ibba; Kwang Won Hong; Dieter Söll

doi:10.1046/j.1365-2443.1996.d01-255.x

Glutaminyl-tRNA synthetase: From genetics to molecular recognition

Michael Ibba, Kwang Won Hong, Dieter Söll

Department of Food Science & Biotechnology

Yale University

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

12 Scopus citations

Abstract

Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They are synthesized by the aminoacyl-tRNA synthetases which select both the correct amino acid and tRNA from a total of more than 400 possible combinations. Genetic, biochemical and structural studies have begun to reveal the mechanisms by which this specificity is achieved by Escherichia coli glutaminyl-tRNA synthetase (GlnRS). Sequence-specific interactions between GlnRS and tRNA^Gln determine both the accuracy of tRNA selection and the efficiency of aminoacylation. Thus, amino acid recognition is tRNA-dependent. Consequently, while a noncognate tRNA may be recognized by GlnRS, the resulting tRNA-enzyme complex displays a considerably reduced affinity for glutamine compared to wild-type. This mechanism now provides a ready explanation as to why the majority of tRNA mischarging events, including those originally described over 25 years ago for GlnRS, impair cellular viability only to a limited degree.

Original language	English
Pages (from-to)	421-427
Number of pages	7
Journal	Genes to Cells
Volume	1
Issue number	5
DOIs	https://doi.org/10.1046/j.1365-2443.1996.d01-255.x
State	Published - 1996

Access to Document

10.1046/j.1365-2443.1996.d01-255.x

Cite this

@article{0d8c51b1afc841bc860b5cf04869b8d5,

title = "Glutaminyl-tRNA synthetase: From genetics to molecular recognition",

abstract = "Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They are synthesized by the aminoacyl-tRNA synthetases which select both the correct amino acid and tRNA from a total of more than 400 possible combinations. Genetic, biochemical and structural studies have begun to reveal the mechanisms by which this specificity is achieved by Escherichia coli glutaminyl-tRNA synthetase (GlnRS). Sequence-specific interactions between GlnRS and tRNAGln determine both the accuracy of tRNA selection and the efficiency of aminoacylation. Thus, amino acid recognition is tRNA-dependent. Consequently, while a noncognate tRNA may be recognized by GlnRS, the resulting tRNA-enzyme complex displays a considerably reduced affinity for glutamine compared to wild-type. This mechanism now provides a ready explanation as to why the majority of tRNA mischarging events, including those originally described over 25 years ago for GlnRS, impair cellular viability only to a limited degree.",

author = "Michael Ibba and Hong, \{Kwang Won\} and Dieter S{\"o}ll",

year = "1996",

doi = "10.1046/j.1365-2443.1996.d01-255.x",

language = "English",

volume = "1",

pages = "421--427",

journal = "Genes to Cells",

issn = "1356-9597",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "5",

}

TY - JOUR

T1 - Glutaminyl-tRNA synthetase

T2 - From genetics to molecular recognition

AU - Ibba, Michael

AU - Hong, Kwang Won

AU - Söll, Dieter

PY - 1996

Y1 - 1996

N2 - Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They are synthesized by the aminoacyl-tRNA synthetases which select both the correct amino acid and tRNA from a total of more than 400 possible combinations. Genetic, biochemical and structural studies have begun to reveal the mechanisms by which this specificity is achieved by Escherichia coli glutaminyl-tRNA synthetase (GlnRS). Sequence-specific interactions between GlnRS and tRNAGln determine both the accuracy of tRNA selection and the efficiency of aminoacylation. Thus, amino acid recognition is tRNA-dependent. Consequently, while a noncognate tRNA may be recognized by GlnRS, the resulting tRNA-enzyme complex displays a considerably reduced affinity for glutamine compared to wild-type. This mechanism now provides a ready explanation as to why the majority of tRNA mischarging events, including those originally described over 25 years ago for GlnRS, impair cellular viability only to a limited degree.

AB - Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They are synthesized by the aminoacyl-tRNA synthetases which select both the correct amino acid and tRNA from a total of more than 400 possible combinations. Genetic, biochemical and structural studies have begun to reveal the mechanisms by which this specificity is achieved by Escherichia coli glutaminyl-tRNA synthetase (GlnRS). Sequence-specific interactions between GlnRS and tRNAGln determine both the accuracy of tRNA selection and the efficiency of aminoacylation. Thus, amino acid recognition is tRNA-dependent. Consequently, while a noncognate tRNA may be recognized by GlnRS, the resulting tRNA-enzyme complex displays a considerably reduced affinity for glutamine compared to wild-type. This mechanism now provides a ready explanation as to why the majority of tRNA mischarging events, including those originally described over 25 years ago for GlnRS, impair cellular viability only to a limited degree.

UR - http://www.scopus.com/inward/record.url?scp=0030133845&partnerID=8YFLogxK

U2 - 10.1046/j.1365-2443.1996.d01-255.x

DO - 10.1046/j.1365-2443.1996.d01-255.x

M3 - Article

C2 - 9078373

AN - SCOPUS:0030133845

SN - 1356-9597

VL - 1

SP - 421

EP - 427

JO - Genes to Cells

JF - Genes to Cells

IS - 5

ER -

Glutaminyl-tRNA synthetase: From genetics to molecular recognition

Abstract

Access to Document

Other files and links

Fingerprint

Cite this