A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase

Anjali P. Mascarenhas; Susan A. Martinis

doi:10.1016/j.febslet.2009.09.039

A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase

Anjali P. Mascarenhas, Susan A. Martinis

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

Abstract

Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is distinct from its aminoacylation domain. Mischarged amino acids are transiently translocated ∼30 Å between active sites for editing by an unknown tRNA-dependent mechanism. A glycine within a flexible β-strand that links the aminoacylation and editing domains of LeuRS was determined to be important to tRNA translocation. The translocation-defective mutation also demonstrated that the editing site screens both correctly and incorrectly charged tRNAs prior to product release.

Original language	English (US)
Pages (from-to)	3443-3447
Number of pages	5
Journal	FEBS Letters
Volume	583
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2009.09.039
State	Published - Nov 3 2009

Keywords

Amino acid editing
Fidelity
Protein synthesis
Translocation

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase",

abstract = "Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is distinct from its aminoacylation domain. Mischarged amino acids are transiently translocated ∼30 {\AA} between active sites for editing by an unknown tRNA-dependent mechanism. A glycine within a flexible β-strand that links the aminoacylation and editing domains of LeuRS was determined to be important to tRNA translocation. The translocation-defective mutation also demonstrated that the editing site screens both correctly and incorrectly charged tRNAs prior to product release.",

keywords = "Amino acid editing, Fidelity, Protein synthesis, Translocation",

author = "Mascarenhas, {Anjali P.} and Martinis, {Susan A.}",

note = "Funding Information: We are grateful to Dr. Stephen Cusack for valuable advice and Drs. Michael Vu and Michal Boniecki for technical and insightful suggestions. This work was supported by the NIH ( GM063789 ). Copyright: Copyright 2011 Elsevier B.V., All rights reserved.",

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AU - Martinis, Susan A.

N1 - Funding Information: We are grateful to Dr. Stephen Cusack for valuable advice and Drs. Michael Vu and Michal Boniecki for technical and insightful suggestions. This work was supported by the NIH ( GM063789 ). Copyright: Copyright 2011 Elsevier B.V., All rights reserved.

PY - 2009/11/3

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N2 - Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is distinct from its aminoacylation domain. Mischarged amino acids are transiently translocated ∼30 Å between active sites for editing by an unknown tRNA-dependent mechanism. A glycine within a flexible β-strand that links the aminoacylation and editing domains of LeuRS was determined to be important to tRNA translocation. The translocation-defective mutation also demonstrated that the editing site screens both correctly and incorrectly charged tRNAs prior to product release.

AB - Aminoacyl-tRNA synthetases often rely on a proofreading mechanism to clear mischarging errors before they can be incorporated into newly synthesized proteins. Leucyl-tRNA synthetase (LeuRS) houses a hydrolytic editing pocket in a domain that is distinct from its aminoacylation domain. Mischarged amino acids are transiently translocated ∼30 Å between active sites for editing by an unknown tRNA-dependent mechanism. A glycine within a flexible β-strand that links the aminoacylation and editing domains of LeuRS was determined to be important to tRNA translocation. The translocation-defective mutation also demonstrated that the editing site screens both correctly and incorrectly charged tRNAs prior to product release.

KW - Amino acid editing

KW - Fidelity

KW - Protein synthesis

KW - Translocation

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A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase

Abstract

Keywords

ASJC Scopus subject areas

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