Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase
The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and pos...
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| Published in: | Molecular cell Vol. 11; no. 4; pp. 951 - 963 |
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| Main Authors: | , , , , , , , , , , , |
| Format: | Journal Article |
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01-04-2003
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| Abstract | The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the α-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis. |
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| AbstractList | The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the alpha-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis. The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the α-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis. |
| Author | Van Den Eynde, Wendy Yaremchuk, Anna Grøtli, Morten Lincecum, Tommie L. Sproat, Brian S. Martinis, Susan A. Van Calenbergh, Serge Tukalo, Michael Mursinna, Richard S. Cusack, Stephen Williams, Amy M. Link, Andreas |
| Author_xml | – sequence: 1 givenname: Tommie L. surname: Lincecum fullname: Lincecum, Tommie L. organization: Department of Biology and Biochemistry, University of Houston, Houston, TX 77204 USA – sequence: 2 givenname: Michael surname: Tukalo fullname: Tukalo, Michael organization: Grenoble Outstation of EMBL, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France – sequence: 3 givenname: Anna surname: Yaremchuk fullname: Yaremchuk, Anna organization: Grenoble Outstation of EMBL, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France – sequence: 4 givenname: Richard S. surname: Mursinna fullname: Mursinna, Richard S. organization: Department of Biology and Biochemistry, University of Houston, Houston, TX 77204 USA – sequence: 5 givenname: Amy M. surname: Williams fullname: Williams, Amy M. organization: Department of Biology and Biochemistry, University of Houston, Houston, TX 77204 USA – sequence: 6 givenname: Brian S. surname: Sproat fullname: Sproat, Brian S. organization: RNA-TEC NV, Minderbroedersstraat 17-19, B-3000 Leuven, Belgium – sequence: 7 givenname: Wendy surname: Van Den Eynde fullname: Van Den Eynde, Wendy organization: RNA-TEC NV, Minderbroedersstraat 17-19, B-3000 Leuven, Belgium – sequence: 8 givenname: Andreas surname: Link fullname: Link, Andreas organization: Institute for Pharmacy, University of Hamburg, Bundesstrasse 45, D-20146 Hamburg, Germany – sequence: 9 givenname: Serge surname: Van Calenbergh fullname: Van Calenbergh, Serge organization: Laboratory of Medicinal Chemistry, Faculty of Pharmacy, University of Gent, Harelbekestraat 72, B-9000 Gent, Belgium – sequence: 10 givenname: Morten surname: Grøtli fullname: Grøtli, Morten organization: Biotechnology Centre of Oslo, University of Oslo, Gaustadalleén 21, N-0349 Oslo, Norway – sequence: 11 givenname: Susan A. surname: Martinis fullname: Martinis, Susan A. email: cusack@embl-grenoble.fr organization: Department of Biology and Biochemistry, University of Houston, Houston, TX 77204 USA – sequence: 12 givenname: Stephen surname: Cusack fullname: Cusack, Stephen email: smartinis@uh.edu organization: Grenoble Outstation of EMBL, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/12718881$$D View this record in MEDLINE/PubMed |
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| Snippet | The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly... |
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| SubjectTerms | Adenosine - analogs & derivatives Adenosine - metabolism Amino Acids - genetics Amino Acids - metabolism Aspartic Acid - genetics Aspartic Acid - metabolism Binding Sites - genetics Leucine-tRNA Ligase - genetics Leucine-tRNA Ligase - metabolism Macromolecular Substances Molecular Conformation Protein Biosynthesis - genetics Proteins - genetics RNA Editing - genetics RNA, Transfer - genetics RNA, Transfer - metabolism |
| Title | Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase |
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