Archaeal minichromosome maintenance (MCM) helicase can unwind DNA bound by archaeal histones and transcription factors.

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TitleArchaeal minichromosome maintenance (MCM) helicase can unwind DNA bound by archaeal histones and transcription factors.
Publication TypeJournal Article
Year of Publication2007
AuthorsShin, J-H, Santangelo, TJ, Xie, Y, Reeve, JN, Kelman, Z
JournalJ Biol Chem
Volume282
Issue7
Pagination4908-15
Date Published2007 Feb 16
ISSN0021-9258
KeywordsAdenosine Triphosphate, Archaeal Proteins, DNA Helicases, DNA Replication, DNA, Archaeal, DNA-Binding Proteins, DNA-Directed RNA Polymerases, Histones, Methanobacteriaceae, TATA-Box Binding Protein, Transcription Factor TFIIB
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.

DOI10.1074/jbc.M606847200
Alternate JournalJ. Biol. Chem.
PubMed ID17158792
Grant ListGM073336-01 / GM / NIGMS NIH HHS / United States