Literature DB >> 10492015

Aminoacyl-tRNA synthetases: a new image for a classical family.

S A Martinis1, P Plateau, J Cavarelli, C Florentz.   

Abstract

The aminoacyl-tRNA synthetases (aaRSs) are a family of enzymes well known for their role in protein synthesis. More recent investigations have discovered that this classic family of enzymes is actually capable of a broad repertoire of functions which not only impact protein synthesis, but extend to a number of other critical cellular activities. Specific aaRSs play roles in cellular fidelity, tRNA processing, RNA splicing, RNA trafficking, apoptosis, transcriptional and translational regulation. A recent EMBO workshop entitled 'Structure and Function of Aminoacyl-tRNA Synthetases' (Mittelwihr, France, October 10-15, 1998), highlighted the diversity of the aaRSs' role within the cell. These novel activities as well as significant advances in delineating mechanisms of substrate specificity and the aminoacylation reaction affirm the family of aaRSs as pharmaceutical targets.

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Year:  1999        PMID: 10492015     DOI: 10.1016/s0300-9084(99)80126-6

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  22 in total

Review 1.  Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process.

Authors:  C R Woese; G J Olsen; M Ibba; D Söll
Journal:  Microbiol Mol Biol Rev       Date:  2000-03       Impact factor: 11.056

2.  The bI4 group I intron binds directly to both its protein splicing partners, a tRNA synthetase and maturase, to facilitate RNA splicing activity.

Authors:  S B Rho; S A Martinis
Journal:  RNA       Date:  2000-12       Impact factor: 4.942

3.  The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.

Authors:  K Galani; H Grosshans; K Deinert; E C Hurt; G Simos
Journal:  EMBO J       Date:  2001-12-03       Impact factor: 11.598

4.  Aminoacyl-tRNA synthetases database Y2K.

Authors:  M Szymanski; J Barciszewski
Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

5.  Crystallization and preliminary X-ray crystallographic study of the wild type and two mutants of the CP1 hydrolytic domain from Aquifex aeolicus leucyl-tRNA synthetase.

Authors:  Vincent Cura; Natacha Olieric; Alexandre Guichard; En-Duo Wang; Dino Moras; Gilbert Eriani; Jean Cavarelli
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-09-13

6.  Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity.

Authors:  Aswini K Betha; Amy M Williams; Susan A Martinis
Journal:  Biochemistry       Date:  2007-05-03       Impact factor: 3.162

7.  Identification and Characterization of Potential Biomarkers by Quantitative Tissue Proteomics of Primary Lung Adenocarcinoma.

Authors:  Chiung-Hung Hsu; Chia-Wei Hsu; Chuen Hsueh; Chih-Liang Wang; Yi-Cheng Wu; Chih-Ching Wu; Chin-Ching Liu; Jau-Song Yu; Yu-Sun Chang; Chia-Jung Yu
Journal:  Mol Cell Proteomics       Date:  2016-05-09       Impact factor: 5.911

8.  An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing.

Authors:  Seung Bae Rho; Tommie L Lincecum; Susan A Martinis
Journal:  EMBO J       Date:  2002-12-16       Impact factor: 11.598

9.  Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase.

Authors:  Manal A Swairjo; Paul R Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2005-01-18       Impact factor: 11.205

10.  Calcium regulates the expression of a Dictyostelium discoideum asparaginyl tRNA synthetase gene.

Authors:  Jyoti K Jaiswal; Vidyanand Nanjundiah
Journal:  J Biosci       Date:  2003-12       Impact factor: 1.826

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