Affinity chromatographic purification of a protein which binds specifically to the yeast leucine tRNA gene.
A crude cell extract from yeast Saccharomyces cerevisae was fractionated by affinity chromatography using the leucine tRNA gene as the recognition site. This approach enables the rapid purification of a protein, which retained its full DNA binding capacity during the enrichment procedure. The active fraction contains two major polypeptides of 140 and 170 kDa and a minor component of 100 kDa. The 170-kDa component does not bind to the DNA. The likelihood that the DNA binding protein is one of the components of transcription factor tau is discussed.
Kaufmann
E
E
MRC Laboratory of Molecular Biology, Cambridge, England.
D001665:Binding Sites; D002846:Chromatography, Affinity / Q000379:methods*; D004258:DNA Polymerase III; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D005800:Genes, Fungal; D008970:Molecular Weight; D011485:Protein Binding; D012356:RNA, Transfer, Leu / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D012356:RNA, Transfer, Leu; D014157:Transcription Factors; C041273:transcription factor tau; D004258:DNA Polymerase III