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J Biol Chem, Vol. 274, Issue 17, 11623-11628, April 23, 1999
From the The active form of transcription termination
factor rho from Escherichia coli is a homohexamer, but
several studies suggest that the six subunits of the hexamer are not
functionally identical. Rho has three tight and three weak ATP binding
sites. Based on our findings, we propose that the tight nucleotide
binding sites are noncatalytic and the weak sites are catalytic. In the
presence of RNA, the rho-catalyzed ATPase rate is fast, close to 30 s
Transcription Termination Factor Rho Contains Three Noncatalytic
Nucleotide Binding Sites
,
Department of Biochemistry, Ohio State
University, Columbus, Ohio 43210 and the § Department of
Genetics and Molecular Biology, Institute for Virus Research, Kyoto
University, Sakyo-ku, Kyoto 606, Japan
1. However, under these conditions the three
tightly bound nucleotides dissociate from the rho hexamer at a slow
rate of 0.02 s1, indicating that the three tight
nucleotide binding sites of rho do not participate in the fast ATPase
turnover. These slowly exchanging nucleotide binding sites of rho are
capable of hydrolyzing ATP, but the resulting products (ADP and
Pi) bind tightly and dissociate from rho about 1500 times
slower than the fast ATPase turnover. Both RNA and excess ATP in
solution are necessary for stabilizing nucleotide binding at these
sites. In the absence of RNA, or when solution ATP is hydrolyzed to
ADP, a faster dissociation of nucleotides was observed. Based on these
results, we propose that the rho hexamer is similar to the
F1-ATPase and T7 DNA helicase-containing noncatalytic sites
that do not participate in the fast ATPase turnover. We propose
that the three tight sites on rho are the noncatalytic sites and
the three weak sites are the catalytic sites.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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