Swapping of three-dimensional domains as a molecular mechanism of dimerization of aminoacyl-tRNA synthetases.
It has been shown recently that many proteins undergo oligomerization through exchange of structural elements. That process, termed a 3D domain swapping, is the replacement of a portion of the tertiary structure of a protein with an identical piece from a second polypeptide chain. When the exchange is reciprocated, domain-swapped dimers embrace with the exchange of elements of secondary structure or domains; however, if the exchange is not reciprocated but propagated along multiple polynucleotide chains, higher-order assemblies may form. In this paper we discuss swapping as a general mechanism of aminoacyl-tRNA synthetases dimerization, specifically plant methionyl-tRNA synthetase.
Deniziak
Marzanna A
MA
Institute of Bioorganic Chemistry of the Polish Academy of Sciences, Poznań.
Barciszewski
Jan
J
D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry*; D016207:Cytokines / Q000737:chemistry; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry; D012275:Oryza / Q000201:enzymology; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016601:RNA-Binding Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D016207:Cytokines; D009363:Neoplasm Proteins; D016601:RNA-Binding Proteins; C077219:small inducible cytokine subfamily E, member 1; D000604:Amino Acyl-tRNA Synthetases