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- W1569124311 abstract "Yeast transcription factor τ interacts with the A and B blocks of the intragenic promoter of tRNA genes. The structure of τ was investigated by identifying the polypeptide chains specifically complexed to the tRNA3Glu gene. Highly purified factor, obtained by an improved purification procedure, contained several polypeptide chains, four of which (Mr = 145,000, 135,000, 100,000 and 65,000) comigrated with τ-DNA complex by polyacrylamide gel electrophoresis. Antibodies raised against the 145- and 100-kDa components altered the migration of τ-DNA complexes in band shift assays and inhibited tRNA synthesis in a reconstituted transcription system. These components are immunologically unrelated proteins. By UV cross-linking to 32P-body-labeled tDNA followed by extensive DNase treatment, two polypeptides of the same size (145 and 100 kDa) were found to be radioactively labeled. Factor τ, therefore, appears to be a multisubunit DNA-binding protein with two distinct polypeptides contributing to DNA recognition. Limited proteolysis of τ generated a protease-resistant τB (τB) domain that binds solely to the B block. τB-tDNA complexes were recognized by anti-145 IgG and contained a 120-kDa polypeptide that could originate from the 145-kDa component by proteolysis. These results strongly suggest that the 145-kDa polypeptide belongs to τB and is responsible for B block binding." @default.
- W1569124311 created "2016-06-24" @default.
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- W1569124311 date "1989-05-01" @default.
- W1569124311 modified "2023-10-10" @default.
- W1569124311 title "Two polypeptide chains in yeast transcription factor τ interact with DNA" @default.
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- W1569124311 doi "https://doi.org/10.1016/s0021-9258(18)83263-x" @default.
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