| Literature DB >> 9600851 |
Abstract
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. Copyright 1998 Academic Press Limited.Entities:
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Year: 1998 PMID： 9600851 DOI： 10.1006/jmbi.1998.1744
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469