PubMed HealthSearch

PubMed · 8255291

Eukaryotic activators function during multiple steps of preinitiation complex assembly.

Abstract

Eukaryotic activator proteins (activators) stimulate transcription by increasing assembly of the preinitiation complex. We have developed methods to quantify the stable assembly of general transcription factors into transcriptional complexes in response to activators. We show that activators function during at least two stages of preinitiation complex assembly: first, to recruit the general transcription factor TFIIB, and then at a second step, after TFIIB entry. It is at this second step that the TATA-box binding protein associated factors act. This step also seems to be critical for activators to stimulate transcription synergistically.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

B Choy, M R Green. 1993-12-09. Eukaryotic activators function during multiple steps of preinitiation complex assembly.. https://doi.org/10.1038/366531a0

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Decoding ALS from the tail end of RNA.

In this issue of Cell Genomics, McKeever et al.1 generate a single-nucleus transcriptomic atlas of ALS/FTLD brain and reveal widespread alternative polyadenylation changes. Their findings highlight 3' end RNA processing as a central integrator of stress responses, cell-type specificity, and disease susceptibility, offering new mechanistic insight and potential therapeutic directions.

Cell Nucleus

Acidification-and-recovery induces nuclear accumulation of neutral red and DNA into human KB oral carcinoma cells.

In cultures of oral cancers, gene transfer has been achieved by delivery systems which introduce DNA into cells but not specifically into the nucleus. We observed that acidification and recovery converted the nuclear-insulated interphase KB carcinoma cells into intense nuclear-accumulating states. Nuclear sequestration of the vital dye neutral red and T7 oligonucleotide was demonstrated qualitatively, and quantitatively by image analysis of single cells. pGem beta gal plasmids of 6.8 kb were introduced into KB cells by similar acidification and recovery pulses. Successful integration into the host KB genome was shown by expression of the lacZ gene of the plasmids. Enhanced nucleo-cytoplasmic transport demonstrated here in KB oral epidermoid carcinoma cells could potentially facilitate gene therapy in oral cancers.

Cell Nucleus

Modulation of the higher-order folding of chromatin by deletion of histone H3 and H4 terminal domains.

The 'tails' of histones H3 and H4 were removed by light in situ trypsin digestion of the nuclei. The alterations in the higher-order folding of chromatin resulting from this treatment were monitored by ethidium bromide titration. We found that DNA-intercalation of ethidium bromide under these conditions exhibited a complex concentration effect that was dependent on the extent of chromatin folding. This most likely reflects the structural transitions of chromatin during its folding as a result of the changes in the nucleosome linker twist [Woodcock, Grigoryev, Horowitz and Whitaker (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 9021-9025]. These results strongly suggest that the H3 and H4 terminal domains play a very important role in chromatin folding. We discuss the molecular basis of this phenomenon and propose a novel generalized model for the higher-order folding of chromatin.

Cell Nucleus