|
|
|
|||||||
|
|||||||||
(Received for publication, May 14, 1997, and in revised form, May 29, 1997)
From the Department of Molecular Biology and Microbiology, School
of Medicine, Case Western Reserve University,
Cleveland, Ohio 44106
Xenopus transcription factor IIIA
(TFIIIA) binds to over 50 base pairs in the internal control region of
the 5 S rRNA gene, yet the binding energy for this interaction
(
Volume 272, Number 32,
Issue of August 8, 1997
pp. 20152-20161
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
G0 = 
12.8 kcal/mol) is no greater than
that exhibited by many proteins that occupy much smaller DNA targets.
Despite considerable study, the distribution of the DNA binding energy
among the various zinc fingers of TFIIIA remains poorly understood. By
analyzing TFIIIA mutants with disruptions of individual zinc fingers,
we have previously shown that each finger contributes favorably to
binding (Del Rio, S., Menezes, S. R., and Setzer, D. R. (1993) J. Mol. Biol. 233, 567-579). Those results also
suggested, however, that simultaneous binding by all nine zinc fingers
of TFIIIA may involve a substantial energetic cost. Using complementary
N- and C-terminal fragments and full-length proteins containing pairs
of disrupted fingers, we now show that energetic interference indeed
occurs between zinc fingers when TFIIIA binds to the 5 S rRNA gene and
that the greatest interference occurs between fingers at opposite ends of the protein in the TFIIIA·5 S rRNA gene complex. Some, but not
all, of the thermodynamically unfavorable strain in the TFIIIA·5 S rRNA gene complex may be derived from bending of the DNA that is
necessary to accommodate simultaneous binding by all nine zinc fingers
of TFIIIA. The energetics of DNA binding by TFIIIA thus emerges as a
compromise between individual favorable contacts of importance along
the length of the internal control region and long range strain or
distortion in the protein, the 5 S rRNA gene, or both that is
necessary to accommodate the various local interactions.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Rothfels, O. Rowland, and J. Segall Zinc fingers 1 and 7 of yeast TFIIIA are essential for assembly of a functional transcription complex on the 5 S RNA gene Nucleic Acids Res., July 10, 2007; (2007) gkm517v1. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. L. Brady, S. N. Ponnampalam, M. J. Bumbulis, and D. R. Setzer Mutations in TFIIIA That Increase Stability of the TFIIIA-5 S rRNA Gene Complex: UNUSUAL EFFECTS ON THE KINETICS OF COMPLEX ASSEMBLY AND DISSOCIATION J. Biol. Chem., July 22, 2005; 280(29): 26743 - 26750. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. L. Brady and D. R. Setzer Is There a Dynamic DNA-Protein Interface in the Transcription Factor IIIA-5 S rRNA Gene Complex? J. Biol. Chem., April 22, 2005; 280(16): 16115 - 16124. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Ghose, M. Malik, and P. W. Huber Restricted Specificity of Xenopus TFIIIA for Transcription of Somatic 5S rRNA Genes Mol. Cell. Biol., March 15, 2004; 24(6): 2467 - 2477. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. M. Fowler, N. J. Greenfield, and J. Moyer Tropomodulin Contains Two Actin Filament Pointed End-capping Domains J. Biol. Chem., October 10, 2003; 278(41): 40000 - 40009. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Schramm and N. Hernandez Recruitment of RNA polymerase III to its target promoters Genes & Dev., October 15, 2002; 16(20): 2593 - 2620. [Full Text] [PDF]
|
|
|
|
|
|
S. Pizzi, G. Dieci, P. Frigeri, G. Piccoli, V. Stocchi, and S. Ottonello Domain Organization and Functional Properties of Yeast Transcription Factor IIIA Species with Different Zinc Stoichiometries J. Biol. Chem., January 22, 1999; 274(4): 2539 - 2548. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |