Stability of human recombinant AIMP1/Р43 protein in complex with tRNA

N. Vorobyova, O. Kornelyuk, D. Lozhko
1 - Taras Shevchenko National University of Kyiv, Kyiv; 2 - Institute of Molecular Biology and Genetics of NASU, Kyiv; 1 - Taras Shevchenko National University of Kyiv, Kyiv; 2 - Institute of Molecular Biology and Genetics of NASU, Kyiv; Institute of Molecular Biology and Genetics of NASU, Kyiv


The interaction of AIMP1/р43 recombinant protein, which is a component of aminoacyl-tRNA synthetase complex in higher eukaryotes, in the complex with tRNA was studied. It was shown that temperature stability of AIMP1/p43 is significantly increased in the complex. Local conformational transition of residue Trp271 of AIMP1/p43, which is associated with intramolecular protein stability, is observed at 430C, but in a complex with tRNA it is observed at 490C. Based on the data of spectrofluorimetric titration the value of the dissociation constant and the
stoichiometry of the complex of AIMP1/p43 with tRNA were determined. The model of the complex of AIMP1/p43 with tRNA was obtained by the
molecular docking method.


AIMP1/р43, tRNA, stabilization, fluorescence spectroscopy

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Glik B. [Molecular Biotechnology. Principles and application]. M. World; 2002. 589 p. Russian

Kordysh MO, Dubrovskyy OL,Kornelyuk AI. [Local conformational transition of Trp125 fluorophore in cytokine EMAP II, induced by physiological temperature]. Physics of live. 2005; 13(1):79-85. Ukrainian

Chen VB, Pettersen EF, Goddard TD, Huang CC, Couch GS. UCSF Chimera – a visualization system for exploratory research and analysis. J Comput Chem. 2004;25(13):1605-1612.

Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005;6(3): 197–208.

Fink AL. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding Dis. 1998;(3): R9-R23.

Francis DM, Page R. Strategies to optimize protein expression in E.сoli. Curr Protoc Protein Sci. 2010;5: 1–29.

Fu Y, Kim Y, Jin KS, Kim HS, [et al.] Structure of the ArgRSGlnRS-AIMP1 complex and its implications for mammalian translation. Proc Natl Acad Sci U S A. 2014;111(42): 15084-9

Ivakhno SS, Kornelyuk AI. Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis. Exp. Oncol. 2004;26(4): 250-5.

Ivanova IuL, Cherni NE, Popenko VI, Filonenko VV, Vartanian OG. Comparative study of localization of tryptophanyl-tRNA-synthetase and components of high molecular weight aminoacyl-tRNA-synthetase complex in animal cells. Mol. Biol. 1993;27(3): 666-84.

Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259): 680- 5.

Murphy RM, Kendrick BS. Protein Misfolding and Aggregation. Biotechnol. Prog. 2007(23):548- 52.

Popenko V I, Ivanova JL, Cherny NE, Filonenko V V, [et al.] Compartmentalization of certain components of the protein synthesis apparatus in mammalian cells. Eur. J. Cell. Biol. 1994;65(1): 60-9.

Quevillon S, Agou F, Robinson J-C, Mirande M. The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine. J. Biol. Chem. 1997;272(51): 32573-9.

Renault L, Kerjan P, Pasqualato S, [et al.] Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry. J. 2001;20(3): 570-8.

Ritchie DW. Evaluation of Protein Docking Predictions Using Hex 3.1 in CAPRI Rounds 1 and 2. PROTEINS: Struct. Funct. Genet. 2003;52: 98-106.

Shalak V, Kaminska M, Mitnacht-Kraus R [et al.] The EMAPII cytokine is released from the mammalian multisynthetase complex after cleavage of its p43/proEMAPII component. J Biol Chem. 2001;


Wolfe CL, Warrington JA, Davis S, Green S, Norcum MT. Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII. Protein Sci. 2003;12(10): 2282-90.

Wright PE, Dyson HJ. Itrinsically unstructured proteins: Reassessing the protein structure-function paradigm. J. Mol. Biol. 1999;293(2): 321-31.



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