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Phenylalanyl-tRNA Synthetase Interacts with DNA: Studies on Activity Using Deoxyribooligonucleotides

K. A. Ivanov*, N. A. Moor, V. N. Ankilova, and O. I. Lavrik

Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, pr. Lavrent'eva 8, Novosibirsk, 630090 Russia; fax: (8-3832) 33-3677; E-mail: ivkon@niboch.nsc.ru

* To whom correspondence should be addressed.

Received February 26, 1999; Revision received July 29, 1999
Phenylalanyl-tRNA synthetase from Thermus thermophilus complexes with short (up to 30 nucleotide length) single-stranded DNA fragments more efficiently than with double-stranded fragments. The complexing between DNA and the protein significantly increases with deoxyribooligonucleotide longer than 20 nucleotides. Using affinity labeling, the binding site of DNA was located near the interface of the alpha- and beta-subunits. The binding sites of DNA and tRNAPhe do not overlap. Phenylalanyl-tRNA synthetase from E. coli also binds DNA.
KEY WORDS: affinity labeling, aminoacyl-tRNA synthetases, Thermus thermophilus