Riding high on the TATA box

Article Abstract:

The three-dimensional molecular arrangement of the TATA-box binding protein (TBP) has been resolved down to the 2.6 angstrom level by Dimitar B. Nikolov and colleagues using X-ray diffraction analysis. TBP, the DNA-binding subunit of the general factor TFIID necessary for RNA polymerase to start genetic transcription, is draped around the DNA molecule like a saddle. Furthermore, the conserved portion of TBP is made up of two indistinguishable 88-89 amino-acid domains. The discovery of TBP's structure is important since this protein is apparently ubiquitous among eukaryotes.

Proteins, DNA binding proteins, Protein structure

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The C-terminal domain of RNA polymerase II couples mRNA processing to transcription

Article Abstract:

Efficient RNA processing requires the carboxy-terminal domain (CTD) of the RNA polymerase II (pol II) large subunit. Truncation of the CTD inhibits splicing, processing of the 3' end and termination of transcription downstream of the poly(A) site. An association between the CTD and 3'-processing factors indicates a site producing messenger RNA (mRNA), which undertakes coupled transcription, splicing and cleavage-polyadenylation of mRNA precursors.

Analysis, RNA polymerases, RNA splicing

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Transcriptional antitermination

Article Abstract:

Mechanisms of antitermination in bacteriophage lambda may provide ways to study similar processes in viruses such as HIV-1 and in eukaryotic genes. Gene expression is controlled by antitermination proteins which can prevent transcriptional termination that would otherwise spread. The N protein in bacteriophage lambda modifies RNA polymerase by inducing the formation of a stable ribonucleo-protein. The lambda Q protein has similar effects on DNA.

Gene expression

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