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<title>2001</title>
<link>https://repository.auw.edu.bd/handle/123456789/840</link>
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<pubDate>Mon, 27 Jul 2026 23:22:56 GMT</pubDate>
<dc:date>2026-07-27T23:22:56Z</dc:date>
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<title>Kinetic trapping of DNA by transcription factor IIIB</title>
<link>https://repository.auw.edu.bd/handle/123456789/1034</link>
<description>Kinetic trapping of DNA by transcription factor IIIB
Mollah, A. K. M. M.
High levels of RNA polymerase III gene transcription are achieved&#13;
by facilitated recycling of the polymerase on transcription factor&#13;
IIIB (TFIIIB)-DNA complexes that are stable through multiple rounds&#13;
&#13;
of initiation. TFIIIB-DNA complexes in yeast comprise the TATA-&#13;
binding protein (TBP), the TFIIB-related factor TFIIIB70, and TFIIIB90.&#13;
&#13;
The high stability of the TFIIIB-DNA complex is conferred by&#13;
TFIIIB90 binding to TFIIIB70-TBP-DNA complexes. This stability is&#13;
thought to result from compound bends introduced in the DNA by&#13;
TBP and TFIIIB90 and by protein–protein interactions that obstruct&#13;
DNA dissociation. Here we present biochemical evidence that the&#13;
high stability of TFIIIB-DNA complexes results from kinetic trapping&#13;
of the DNA. Thermodynamic analysis shows that the free energies&#13;
of formation of TFIIIB70-TBP-DNA (DG° 5 212.10 6 0.12 kcalymol)&#13;
and TFIIIB-DNA (DG° 5 211.90 6 0.14 kcalymol) complexes are&#13;
equivalent whereas a kinetic analysis shows that the half-lives of&#13;
these complexes (46 6 3 min and 95 6 6 min, respectively) differ&#13;
&#13;
significantly. The differential stability of these isoenergetic com-&#13;
plexes demonstrates that TFIIIB90 binding energy is used to drive&#13;
&#13;
conformational changes and increase the barrier to complex&#13;
dissociation.
</description>
<pubDate>Mon, 01 Jan 2001 00:00:00 GMT</pubDate>
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<dc:date>2001-01-01T00:00:00Z</dc:date>
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