The phenylalanyl-tRNA synthetase specifically binds DNA.
The phenylalanyl-tRNA synthetase (FRS) from Thermus thermophilus is modularly composed of several different domains, some of which are not required for aminoacylation. In particular, the enzyme has the structural prerequisites for a DNA-binding protein. We demonstrate by gel retardation and competition experiments that the FRS specifically binds certain DNA sequences of the T. thermophilus genomic DNA. Although the implication of this finding is not yet understood, increasing evidence indicates an alternative function of this enzyme not related to aminoacylation. This might be a fundamental cellular process involved in cell proliferation which is related in bacteria and in humans.
Lechler
A
A
Laboratorium für Biochemie, Universität Bayreuth, Universitätsstrasse 30, Bayreuth, 95440, Germany.
Kreutzer
R
R
D000215:Acylation; D000596:Amino Acids / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism*; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D011485:Protein Binding; D013379:Substrate Specificity; D016963:Thermus thermophilus
D000596:Amino Acids; D004269:DNA, Bacterial; D010652:Phenylalanine-tRNA Ligase