Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure.

Literature DB >> 2014166

Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure.

Abstract

The gene coding for E. coli cysteinyl-tRNA synthetase (cysS) was isolated by complementation of a strain deficient in cysteinyl-tRNA synthetase activity at high temperature (43 degrees C). Sequencing of a 2.1 kbp DNA fragment revealed an open reading frame of 1383 bp coding for a protein of 461 amino acid residues with a Mr of 52,280, a value in close agreement with that observed for the purified protein, which behaves as a monomer. The sequence of CysRS bears the canonical His-Ile- Gly -His (HIGH) and Lys-Met-Ser-Lys-Ser (KMSKS) motifs characteristic of the group of enzymes containing a Rossmann fold; furthermore, it shows striking homologies with MetRS (an homodimer of 677 residues) and to a lesser extent with Ile-, Leu-, and ValRS (monomers of 939, 860, and 951 residues respectively). With its monomeric state and smaller size, CysRS is probably more closely related to the primordial aminoacyl-tRNA synthetase from which all have diverged.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 1991 PMID： 2014166 PMCID： PMC333589 DOI： 10.1093/nar/19.2.265

Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971

27 in total

10. Intron locations and functional deletions in relation to the design and evolution of a subgroup of class I tRNA synthetases.

Authors: P Schimmel; A Shepard; K Shiba
Journal: Protein Sci Date: 1992-10 Impact factor: 6.725

Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure.

1. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.

2. The subunit structure of methionyl-tRNA synthetase from Escherichia coli.

3. Cloning and characterization of the gene for Escherichia coli tryptophanyl-transfer ribonucleic acid synthetase.

4. Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product.

5. The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene.

6. Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution.

7. Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases.

8. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.

9. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene.

10. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase.

Review 1. On the evolution of structure in aminoacyl-tRNA synthetases.

2. Functional annotation of class I lysyl-tRNA synthetase phylogeny indicates a limited role for gene transfer.

3. A statistical test of hypotheses on the organization and origin of the genetic code.

4. Functional assembly of a randomly cleaved protein.

5. New nucleotide sequence data on the EMBL File Server.

6. An important 2'-OH group for an RNA-protein interaction.

7. A comparison of several similarity indices used in the classification of protein sequences: a multivariate analysis.

8. Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.

9. Evolution and relatedness in two aminoacyl-tRNA synthetase families.

10. Intron locations and functional deletions in relation to the design and evolution of a subgroup of class I tRNA synthetases.