Abstract
By measuring steady-state rates of dinucleotide synthesis on double-stranded (d.s.) and partially single-stranded (p.s.s.) promoters, and topological unwinding due to open complex formation on plasmids, we have obtained evidence that open complex formation in bacteriophage T7 RNA polymerase:promoter binary complexes is thermodynamically disfavored and that the rate of collapse of the open complex is competitive with the rate of transcription initiation. It is suggested that open complex instability is a kinetic mechanism that allows T7 RNA polymerase (RNAP) to achieve promoter specificity while still allowing for efficient promoter release. Open complex instability could also provide a mechanism for modulating the K(M) for the initiating NTPs so as to allow different promoters to respond differently to physiological changes in NTP concentration.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 958-977 |
| Number of pages | 20 |
| Journal | Journal of Molecular Biology |
| Volume | 273 |
| Issue number | 5 |
| DOIs | |
| State | Published - Nov 14 1997 |
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Keywords
- Open complex
- Promoters
- T7 RNA polymerase
- Transcription initiation
ASJC Scopus subject areas
- Virology
Cite this
Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase. / Villemain, Jana; Guajardo, Richard; Sousa, Rui J.
In: Journal of Molecular Biology, Vol. 273, No. 5, 14.11.1997, p. 958-977.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Role of open complex instability in kinetic promoter selection by bacteriophage T7 RNA polymerase
AU - Villemain, Jana
AU - Guajardo, Richard
AU - Sousa, Rui J
PY - 1997/11/14
Y1 - 1997/11/14
N2 - By measuring steady-state rates of dinucleotide synthesis on double-stranded (d.s.) and partially single-stranded (p.s.s.) promoters, and topological unwinding due to open complex formation on plasmids, we have obtained evidence that open complex formation in bacteriophage T7 RNA polymerase:promoter binary complexes is thermodynamically disfavored and that the rate of collapse of the open complex is competitive with the rate of transcription initiation. It is suggested that open complex instability is a kinetic mechanism that allows T7 RNA polymerase (RNAP) to achieve promoter specificity while still allowing for efficient promoter release. Open complex instability could also provide a mechanism for modulating the K(M) for the initiating NTPs so as to allow different promoters to respond differently to physiological changes in NTP concentration.
AB - By measuring steady-state rates of dinucleotide synthesis on double-stranded (d.s.) and partially single-stranded (p.s.s.) promoters, and topological unwinding due to open complex formation on plasmids, we have obtained evidence that open complex formation in bacteriophage T7 RNA polymerase:promoter binary complexes is thermodynamically disfavored and that the rate of collapse of the open complex is competitive with the rate of transcription initiation. It is suggested that open complex instability is a kinetic mechanism that allows T7 RNA polymerase (RNAP) to achieve promoter specificity while still allowing for efficient promoter release. Open complex instability could also provide a mechanism for modulating the K(M) for the initiating NTPs so as to allow different promoters to respond differently to physiological changes in NTP concentration.
KW - Open complex
KW - Promoters
KW - T7 RNA polymerase
KW - Transcription initiation
UR - http://www.scopus.com/inward/record.url?scp=0031567783&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031567783&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1997.1358
DO - 10.1006/jmbi.1997.1358
M3 - Article
C2 - 9367784
AN - SCOPUS:0031567783
VL - 273
SP - 958
EP - 977
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 5
ER -