On ARS-interacting multifunctional protein p18

Viktor Deineko

doi:10.1038/npre.2008.1593.1

Abstract

AbstractNine aminoacyl-tRNA synthetases with three auxiliary components are forming a multisynthetase complex which is essential component of protein biosynthesis machinery. The smallest auxiliary component p18 takes part in biosynthesis channeling. It is also a regulator of p53 and has tumor suppressing function. Particular structure of this protein is still unknown. Here methods of structural bioinformatics were applied to generate a model of p18 spatial structure suitable for further research. The structure was created using homology modeling. DNA-binding residues of p18 were also derived both from raw sequence and from three-dimensional structure model.

Highlights

IntroductionAminoacyl-tRNA synthetases are essential enzymes that catalyze ligation of specific amino acids to cognate tRNAs. Aminoacyl-tRNA synthetases are essential enzymes that catalyze ligation of specific amino acids to cognate tRNAs
Aminoacyl-tRNA synthetases are essential enzymes that catalyze ligation of specific amino acids to cognate tRNAs.They carrying on some non-enzymatic functions
It was shown that it demonstrates strong sequence similarity both with glutathione S-transferase and subunits β and γ of elongation factor 1 [10]

Summary

Introduction

Aminoacyl-tRNA synthetases are essential enzymes that catalyze ligation of specific amino acids to cognate tRNAs. Aminoacyl-tRNA synthetases are essential enzymes that catalyze ligation of specific amino acids to cognate tRNAs In eukaryotes nine aminoacyltRNA synthetases in assotiation with 3 auxiliary components form a multienzyme complex. Despite the fact that multisynthetase complex was studied over 20 years a role of different components and overall process of assemblage are still hypothesized. Participation of auxiliary proteins in synthetase gathering is an issue of particular interest. Multifunctional Protein 3 (AIMP3) is the smallest non-enzymatic component of multisynthetase complex[6,7]. This protein is less studied among other auxiliary components. It was shown that it demonstrates strong sequence similarity both with glutathione S-transferase and subunits β and γ of elongation factor 1 [10]

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