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Nucleic Acids Research, 1990, Vol. 18, No. 17 5055-5062
© 1990

MOLECULAR BIOLOGY

The effects of disrupting 5S RNA helical structures on the binding of Xenopus transcription factor IIIA

Qimin You and Paul J. Romaniuk*

Department of Biochemistry and Microbiology, University of Victoria PO Box 3055, Victoria, BC V8W 3P6, Canada

*To whom correspondence should be addressed

Received June 12, 1990. Revised August 1, 1990. Accepted August 1, 1990.

Block mutations were constructed in helical stems II, III, IV and V of Xenopus laevis oocyte 5S RNA. The affinities of these mutants for binding to transcription factor IIIA (TFIIIA) were determined using a nitrocellulose filter binding assay. Mutations in stems III and IV had little or no effect on the binding affinity of TFIIIA for 5S RNA. However, single mutants in stems II and V (positions 16–21, 57–62, 71–72, and 103–104) which disrupt the double helix, reduce the binding of TFIIIA by a factor of two to three fold. In contrast, double mutants (16–21/57–62, 71–72/103–104) which restore the helical structure of these stems, but with altered sequences, fully restore the TFIIIA binding affinity. The experiments reported here indicate that the double helical structures of stems II and V, but not the sequences, are required for optimal TFIIIA binding.


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Home page
 J. Biol. Chem.Home page
S. L. Rawlings, G. D. Matt, and P. W. Huber
Analysis of the Binding of Xenopus Transcription Factor IIIA to Oocyte 5 S rRNA and to the 5 S rRNA Gene
J. Biol. Chem., January 12, 1996; 271(2): 869 - 877.
[Abstract] [Full Text] [PDF]


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