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Validated All-in-One™ qPCR Primer for UBTF(NM_014233.4) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
Upstream binding factor (UBF) is a transcription factor required for expression of the 18S, 5.8S, and 28S ribosomal RNAs, along with SL1 (a complex of TBP (MIM 600075) and multiple TBP-associated factors or 'TAFs'). Two UBF polypeptides, of 94 and 97 kD, exist in the human (Bell et al., 1988 [PubMed 3413483]). UBF is a nucleolar phosphoprotein with both DNA binding and transactivation domains. Sequence-specific DNA binding to the core and upstream control elements of the human rRNA promoter is mediated through several HMG boxes (Jantzen et al., 1990 [PubMed 2330041]).[supplied by OMIM].
Gene References into function
- The three-dimensional solution structure of the first high mobility group (HMG) box domain in upstream binding factor has been determined by multidimensional NMR.
- we have identified an interaction between UBF and TAF1, a factor involved in the transcription of cell cycle and growth regulatory genes. Coimmunoprecipitation and protein-protein interaction assays confirmed that TAF1 binds to UBF.
- The DNA binding affinity of UBF's fifth box domain (HMG box 5) is found to be much weaker than that of the first HMG box domain (HMG box 1).
- Data show that both UBF1 and UBF2 activate RNA polymerase II-regulated, beta-catenin-responsive promoters.
- Proto-Oncogene Proteins c-myc activated transcription from the UBF promoter
- results suggest that extensive binding of UBF is responsible for formation and maintenance of the secondary constriction at active NORs, and that UBF mediates recruitment of the pol I machinery to nucleoli independently of promoter elements
- Data suggest that the A state of human upstream binding factor HMG Box1 could represent a potential folding intermediate on protein folding pathway.
- A potential protein-folding pathway is proposed for upstream binding factor HMG box 1 domain based on the early stages of its pH 2.1 unfolded state characterized by multidimensional heteronuclear magnetic resonance spectroscopy.
- SL1 directs preinitiation complex formation, functioning in core promoter binding, RNA polymerase I recruitment, and UBF stabilization.
- model for CAST/hPAF49 function in which the network of interactions of Pol I-specific subunits with UBF facilitates conformational changes of the polymerase, leading to stabilization of the Pol I-template complex and, thereby, activation of transcription
- UBF activates transcription in the transition between initiation and elongation, at promoter escape by RNA polymerase I (Pol I).
- Upon p14ARF overexpression, UBF was found hypophosphorylated, thus unable to efficiently recruit the transcription complex, these data define a new p53-independent pathway that could regulate cell cycle through the negative control of rRNA transcription.
- GdmCl-induced equilibrium unfolding transition of HMG box 5 of hUBF was monitored by both circular dichroism and fluorescence spectra. A cooperative two-state unfolding process was observed
- possible sites in hUBF HMG box 5 that may interact with the first bromodomain of TAF1 were proposed
- transcription factor UBF binds extensively across rDNA throughout the cell cycle, resulting in a specialized form of chromatin that is the hallmark of active nucleolar organizer regions
- found a small but significant difference between the emerging daughter cells in the number of UBF-loaded NORs
- The authors propose that UBF is recruited to the replication compartments to aid replication of HSV-1 DNA.