TY - JOUR
T1 - Archaeal minichromosome maintenance (MCM) helicase can unwind DNA bound by archaeal histones and transcription factors
AU - Shin, Jae Ho
AU - Santangelo, Thomas J.
AU - Xie, Yunwei
AU - Reeve, John N.
AU - Kelman, Zvi
PY - 2007/2/16
Y1 - 2007/2/16
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33947545128&partnerID=8YFLogxK
U2 - 10.1074/jbc.M606847200
DO - 10.1074/jbc.M606847200
M3 - Article
C2 - 17158792
AN - SCOPUS:33947545128
SN - 0021-9258
VL - 282
SP - 4908
EP - 4915
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -