Journal Article

Dimerization and HMG box domains 1–3 present in <i>Xenopus</i> UBF are sufficient for its role in transcriptional enhancement

Gareth J. Sullivan and Brian McStay

in Nucleic Acids Research

Volume 26, issue 15, pages 3555-3561
Published in print August 1998 | ISSN: 0305-1048
Published online August 1998 | e-ISSN: 1362-4962 | DOI: https://dx.doi.org/10.1093/nar/26.15.3555
Dimerization and HMG box domains 1–3 present in Xenopus UBF are sufficient for its role in transcriptional enhancement

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Transcription of Xenopus ribosomal genes by RNA polymerase I is directed by a stable transcription complex that forms on the gene promoter. This complex is comprised of the HMG box factor UBF and the TBP-containing complex Rib1. Repeated sequence elements found upstream of the ribosomal gene promoter act as RNA polymerase I-specific transcriptional enhancers. These enhancers function by increasing the probability of a stable transcription complex forming on the adjacent promoter. UBF is required for enhancer function. This role in enhancement is distinct from that at the promoter and does not involve translocation of UBF from enhancer repeats to the promoter. Here we utilize an in vitro system to demonstrate that a combination of the dimerization domain of UBF and HMG boxes 1–3 are sufficient to specify its role in enhancement. We also demonstrate that the acidic C-terminus of UBF is primarily responsible for its observed interaction with Rib1. Thus, we have uncoupled the Rib1 interaction and enhancer functions of UBF and can conclude that direct interaction with Rib1 is not a prerequisite for the enhancer function of UBF.

Journal Article.  5596 words.  Illustrated.

Subjects: Chemistry ; Biochemistry ; Bioinformatics and Computational Biology ; Genetics and Genomics ; Molecular and Cell Biology

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