Search for Functionally Significant Motifs and Amino Acid Residues of Actin

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...

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Bibliographic Details
Published in:Molecular biology (New York) 2018, Vol.52 (1), p.118-135
Main Authors: Tikhomirova, T. S., Ievlev, R. S., Suvorina, M. Yu, Bobyleva, L. G., Vikhlyantsev, I. M., Surin, A. K., Galzitskaya, O. V.
Format: Article
Language:English
Subjects:
Actin
Amino acid sequence
Amino acids
Amyloidogenesis
Binding sites
Biochemistry
Bioinformatics
Biomedical and Life Sciences
Cytoskeleton
High-performance liquid chromatography
Human Genetics
Life Sciences
Liquid chromatography
Mass spectrometry
Mass spectroscopy
Molecular modelling
Protein interaction
Residues
Structure-function relationships
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Summary: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.
ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893318010193