Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases | Zendy

Deniziak Marzanna A. | Zendy; Barciszewski Jan | Zendy

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Swapping of Three‐Dimensional Domains as a Molecular Mechanism of Dimerization of Aminoacyl‐tRNA Synthetases

Author(s) -

Deniziak Marzanna A.,

Barciszewski Jan

Publication year - 2002

Publication title -

iubmb life

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.132

H-Index - 113

eISSN - 1521-6551

pISSN - 1521-6543

DOI - 10.1080/15216540214313

Subject(s) - aminoacyl trna synthetase , transfer rna , amino acyl trna synthetases , polynucleotide , mechanism (biology) , chemistry , domain (mathematical analysis) , biochemistry , stereochemistry , biology , rna , gene , physics , mathematical analysis , mathematics , quantum mechanics

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.

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