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Papers In Press, published online ahead of print October 29, 2001
J. Biol. Chem, 10.1074/jbc.M108924200
Submitted on September 17, 2001
Revised on October 25, 2001
Accepted on October 29, 2001
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461
Corresponding Author: willis{at}aecom.yu.edu
An important step in the assembly of RNA polymerase (pol) III transcription complexes on tRNA and 5S genes is the interaction between the tetratricopeptide repeat (TPR)-containing subunit of TFIIIC (TFIIIC131) and the TFIIB-related subunit of TFIIIB (TFIIIB70/Brf1). A fragment of TFIIIC131 that contains the hydrophilic amino-terminus and two TPR arrays, with 5 and 4 repeats respectively (Nt-TPR9), is sufficient to support an interaction with TFIIIB70. Here we evaluate the contribution of each TPR array to TFIIIB70 binding. Both TPR arrays bind independently to TFIIIB70 with TPR6-9 having a four-fold higher apparent affinity than TPR1-5. However, the TPR arrays are not sufficient for a high affinity interaction with TFIIIB70. The addition of amino-terminal sequences increases the affinity of TPR1-5 18-fold to create a high affinity TFIIIB70 binding site (Nt-TPR5, 44 ± 6 nM). Although the Nt-TPR5 and TPR6-9 fragments are contained entirely within the Nt-TPR9 fragment, the affinity of the latter is significantly lower than either of these smaller fragments. The results demonstrate that the TFIIIB70 binding sites in TFIIIC131 are subject to autoinhibition. We propose that the binding of TFIIIB70 to these sites within the TFIIIC complex may proceed in an ordered fashion.
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