Phenylalanyl-tRNA synthetase interacts with DNA: studies on activity using deoxyribooligonucleotides.
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.
Ivanov
K A
KA
Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia. ivkon@niboch.nsc.ru
Moor
N A
NA
Ankilova
V N
VN
Lavrik
O I
OI
D004247:DNA / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism*; D003854:Deoxyribonucleotides / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D009841:Oligonucleotides / Q000378:metabolism*; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D019920:Photoaffinity Labels; D012343:RNA, Transfer / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology; D014158:Transcription, Genetic
D004277:DNA, Single-Stranded; D003854:Deoxyribonucleotides; D009841:Oligonucleotides; D019920:Photoaffinity Labels; D004247:DNA; D012343:RNA, Transfer; D010652:Phenylalanine-tRNA Ligase