TY - JOUR
T1 - Structural basis of transcription initiation
T2 - An RNA polymerase holoenzyme-DNA complex
AU - Murakami, Katsuhiko S.
AU - Masuda, Shoko
AU - Campbell, Elizabeth A.
AU - Muzzin, Oriana
AU - Darst, Seth A.
PY - 2002/5/17
Y1 - 2002/5/17
N2 - The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (α2ββ′ωσA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel All sequence-specific contacts with core promoter elements are mediated by the subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the or subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced-10 and -35 elements and provides the basis for models of the closed and open promoter complexes.
AB - The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (α2ββ′ωσA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel All sequence-specific contacts with core promoter elements are mediated by the subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the or subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced-10 and -35 elements and provides the basis for models of the closed and open promoter complexes.
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U2 - 10.1126/science.1069595
DO - 10.1126/science.1069595
M3 - Article
C2 - 12016307
AN - SCOPUS:0037123602
SN - 0036-8075
VL - 296
SP - 1285
EP - 1290
JO - Science
JF - Science
IS - 5571
ER -