Expression of rat aspartyl-tRNA synthetase in Saccharomyces cerevisiae. Role of the NH2-terminal polypeptide extension on enzyme activity and stability (Q71763445)

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scientific article published on 01 November 1996

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English	Expression of rat aspartyl-tRNA synthetase in Saccharomyces cerevisiae. Role of the NH2-terminal polypeptide extension on enzyme activity and stability	scientific article published on 01 November 1996

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21 October 2019

Expression of rat aspartyl-tRNA synthetase in Saccharomyces cerevisiae. Role of the NH2-terminal polypeptide extension on enzyme activity and stability (English)

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21 October 2019

Saccharomyces cerevisiae

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F Agou

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21 October 2019

J P Waller

2

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21 October 2019

M Mirande

3

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21 October 2019

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1 November 1996

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21 October 2019

Journal of Biological Chemistry

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21 October 2019

271

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21 October 2019

46

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21 October 2019

29295-29303

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21 October 2019

Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs

1 reference

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Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

1 reference

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Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate

1 reference

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The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli

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Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

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Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP

1 reference

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Functional dissection of a predicted class-defining motif in a class II tRNA synthetase of unknown structure.

1 reference

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Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline

1 reference

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A single substitution in the motif 1 of Escherichia coli lysyl-tRNA synthetase induces cooperativity toward amino acid binding

1 reference

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Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen

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Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase

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Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex

1 reference

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Maximizing the expression of mammalian cytochrome P-450 monooxygenase activities in yeast cells

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DNA sequencing with chain-terminating inhibitors

1 reference

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Macromolecular Complexes of Aminoacyl-tRNA Synthetases from Eukaryotes. 1.Extensive Purification and Characterization of the High-Molecular-Weight Complex(es) of Seven Aminoacyl-tRNA Synthetases from Sheep Liver

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Foreign gene expression in yeast: a review

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Multiple forms of arginyl- and lysyl-tRNA synthetases in rat liver: a re-evaluation

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Specificity of cotranslational amino-terminal processing of proteins in yeast

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Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.

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Purification and characterization of the isoleucyl-tRNA synthetase component from the high molecular weight complex of sheep liver: a hydrophobic metalloprotein

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21 January 2018

Cytoplasmic aspartyl-tRNA synthetase from Saccharomyces cerevisiae. Study of its functional organisation by deletion analysis

1 reference

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Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins

1 reference

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21 January 2018

The polyanion-binding domain of cytoplasmic Lys-tRNA synthetase from Saccharomyces cerevisiae is not essential for cell viability

1 reference

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21 January 2018

Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase

1 reference

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21 January 2018

The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)

1 reference

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21 January 2018

Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases.

1 reference

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21 January 2018

Identifiers

10.1074/JBC.271.46.29295

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910590%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8910590%20AND%20SRC:MED&resulttype=core&format=json

21 October 2019

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