PMID:8643363: Difference between revisions

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!align=left  |Citation
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'''Liu, H , Yap, LP , Stehlin, C  and Musier-Forsyth, K '''  (1995) Molecular recognition of tRNA(Pro) by Escherichia coli proline-tRNA synthetase. ''Nucleic Acids Symp. Ser.'' '''''':176-8
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!align=left  |Abstract
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We have investigated the molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase (ProRS) in vitro using semi-synthetic tRNAs and site-directed mutagenesis of full-length tRNA transcripts. These studies have led to an improved understanding of how this class II synthetase interacts with its tRNA substrate. The ability to efficiently aminoacylate a tRNA(Pro) molecule assembled by annealing together a shorter, chemically synthesized oligonucleotide and a 3/4 tRNA prepared enzymatically, has facilitated the identification of RNA structural features that are critical for aminoacylation by ProRS. This approach has been successful using either a 3'-3/4 tRNA annealed to a 5'-oligonucleotide or a 5'-3/4 tRNA annealed to a 3'-oligonucleotide. These studies show that ProRS appears to be particularly sensitive to mutations that result in structural changes in the core region of tRNA(Pro). Moreover, the so-called "variable pocket" nucleotides appear to be dispensable for aminoacylation. We have also identified a specific 2'-hydroxyl-base interaction between the ribose of U8 and the 2-amino group of G46 that makes a thermodynamically significant contribution to tRNA(Pro) aminoacylation by E. coli ProRS.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8643363 PubMed]
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!align=left  |Keywords
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Amino Acyl-tRNA Synthetases/metabolism; Base Sequence; Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Hydroxylation; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RNA, Transfer, Pro/chemistry; RNA, Transfer, Pro/genetics; RNA, Transfer, Pro/metabolism; Thermodynamics
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==Significance {{HelpIcon|Help:Literature}} ==
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}
==Annotations {{HelpIcon|Help:Literature}}==
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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Revision as of 14:41, 12 January 2013

Citation

'Liu, H , Yap, LP , Stehlin, C and Musier-Forsyth, K (1995) Molecular recognition of tRNA(Pro) by Escherichia coli proline-tRNA synthetase. Nucleic Acids Symp. Ser. ':176-8

Abstract

We have investigated the molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase (ProRS) in vitro using semi-synthetic tRNAs and site-directed mutagenesis of full-length tRNA transcripts. These studies have led to an improved understanding of how this class II synthetase interacts with its tRNA substrate. The ability to efficiently aminoacylate a tRNA(Pro) molecule assembled by annealing together a shorter, chemically synthesized oligonucleotide and a 3/4 tRNA prepared enzymatically, has facilitated the identification of RNA structural features that are critical for aminoacylation by ProRS. This approach has been successful using either a 3'-3/4 tRNA annealed to a 5'-oligonucleotide or a 5'-3/4 tRNA annealed to a 3'-oligonucleotide. These studies show that ProRS appears to be particularly sensitive to mutations that result in structural changes in the core region of tRNA(Pro). Moreover, the so-called "variable pocket" nucleotides appear to be dispensable for aminoacylation. We have also identified a specific 2'-hydroxyl-base interaction between the ribose of U8 and the 2-amino group of G46 that makes a thermodynamically significant contribution to tRNA(Pro) aminoacylation by E. coli ProRS.

Links

PubMed

Keywords

Amino Acyl-tRNA Synthetases/metabolism; Base Sequence; Binding Sites; Escherichia coli/genetics; Escherichia coli/metabolism; Hydroxylation; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RNA, Transfer, Pro/chemistry; RNA, Transfer, Pro/genetics; RNA, Transfer, Pro/metabolism; Thermodynamics

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Significance

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Useful Materials and Methods

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Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status
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