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A more recent version of this article appeared on August 9, 2002
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M111009200v1
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Papers In Press, published online ahead of print May 28, 2002
J. Biol. Chem, 10.1074/jbc.M111009200
Submitted on November 16, 2001
Revised on May 23, 2002
Accepted on May 28, 2002

Mutations in Rho transcription termination factor Rho that affect RNA tracking

Yi Xu, Harold Kohn, and William R. Widger

Biology and Biochemistry, University of Houston, Houston, TX 77204

Corresponding Author: widger{at}uh.edu

Model studies have identified 16 conserved positively charged amino acids that form a positive strip pointing towards the center hole of Rho. Fourteen residues were individually changed to either an alanine or a glycine and one to a glutamate. Residues R269, R272, K283, R296, K298, and R299 form a subdomain (locus) located N-terminal to (above) the ATP hydrolysis domain (P-loop) and mutations in these residues led to either inactive Rho or to proteins displaying decreased kcat for poly(C)-dependent ATP hydrolysis, increased KM for ribo(C)10 activation, and decreased transcription termination efficiencies (57 to 77 %) compared with wild-type Rho. Residues R347, K348, K352, and R353 form a subdomain (locus) C-terminal to (below) the ATP hydrolysis domain, and mutations in these residues also show a decreased kcat for poly(C)-dependent ATP hydrolysis, an increased KM for ribo(C)10 activation, and a 50 to 70% decrease in transcription termination, compared with wild-type Rho. Residues R212 and K336 surround the ATP hydrolysis domain, and mutations in these residues also altered the kinetic properties of Rho. We conclude that the secondary RNA tracking site consists of amino acids whose putative orientation faces the central hole in Rho and in part reside in two clusters of positively charged residues located above and below the ATP hydrolysis domain.


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