2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 52(2018) N 1 p. 118-135; DOI 10.1134/S0026893318010193 Full Text

T.S. Tikhomirova1,2, R.S. Ievlev1, M.Yu. Suvorina1, L.G. Bobyleva3, I.M. Vikhlyantsev3,4, A.K. Surin1,5, O.V. Galzitskaya1*

Search for Functionally Significant Motifs and Amino Acid Residues of Actin

1Institute of Protein Research, Russian Academy of Science, Pushchino, Moscow oblast, 142290 Russia
2Institute for Biological Instrumentation, Russian Academy of Science, Pushchino, Moscow oblast, 142290 Russia
3Institute of Theoretical and Experimental Biophysics, Russian Academy of Science, Pushchino, Moscow oblast, 142290 Russia
4Pushchino State Institute of Natural Science, Pushchino, Moscow oblast, 142290 Russia
5State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow oblast, 142279 Russia

Received - 2017-06-02; Accepted - 2017-06-30

The scientific interest to the structural and functional properties of actin is determined by its abundance in cells. Being an important component of the cytoskeleton, actin is involved in many protein-protein interactions. Using crystal structures and molecular models, we have mapped the amino acid residues that are involved in these interactions and form the ATP-binding site of the actin monomer. Moreover, using mass spectrometry and high-performance liquid chromatography methods, we have discovered the regions of the amino acid sequence of actin that form the core of the actin fibril. According to the bioinformatic analysis, these regions are amyloidogenic and are located in the C-terminal region and in the hinge between the first and third subdomains. The data obtained are applicable to chordate actin, because multiple alignment revealed highly conserved amino acid sequences. In turn, the comparison of the chordate actin with the bacterial homologs showed the presence of numerous amino acid substitutions and insertions.

actin, multiple alignment, fibril actin, mass spectrometry