The purification and properties of a double-stranded DNA-binding protein encoded by the gene D5 of bacteriophage T5.

作者: A.C. Rice , T.A. Ficht , L.A. Holladay , R.W. Moyer

DOI: 10.1016/S0021-9258(18)36048-4

关键词:

摘要: We have purified a DNA-binding protein from bacteriophage T5-infected cells. The is the product of T5 gene D5 and produced in quantities ultimately exceeding 2% total cell protein. has no tendency to aggregate exists solution as monomer about 29,000 daltons. Although binds with high affinity both single-stranded (fd, T7) duplex DNA (T5, T7), there preferred binding DNA. cooperative an estimated dissociation constant 6.27 x 10(-10) M leads production more condensed form In contrast, noncooperative only 1.85 10(-8) produces sedimentation shift proportional added mass known be required for replication inhibition early phage expression. also show here that initiate transcription late region genome.

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