| Literature DB >> 17158792 |
Jae-Ho Shin1, Thomas J Santangelo2, Yunwei Xie2, John N Reeve2, Zvi Kelman3.
Abstract
Protein-DNA complexes must be disassembled to facilitate DNA replication. Replication forks contain a helicase that unwinds the duplex DNA at the front of the fork. The minichromosome maintenance helicase from the archaeon Methanothermobacter thermautotrophicus required only ATP to unwind DNA bound into complexes by the M. thermautotrophicus archaeal histone HMtA2, transcription repressor TrpY, or into a transcription pre-initiation complex by M. thermautotrophicus TATA-box-binding protein, transcription factor B, and RNA polymerase. In contrast, the minichromosome maintenance helicase was unable to unwind DNA bound by this archaeal RNA polymerase in a stalled transcript-elongating complex.Entities:
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Year: 2006 PMID: 17158792 DOI: 10.1074/jbc.M606847200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157