Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription

Article Abstract:

Phosphorylated forms of RNA polymerase II and associated mRNA processing factors have been studied during transcription. Results indicate a possible dynamic association of mRNA processing factors with forms of the polymerase modified in various ways all through the transcription cycle.

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Capping, splicing, and 3' processing are independently stimulated by RNA polymerase II: different functions for different segments of the CTD

Article Abstract:

Differing functions for different segments of the carboxy-terminal domain (CTD) in pre-mRNA processing are discussed. Splicing, capping, and 3' processing, the three major pre-mRNA processing steps, have been found to be stimulated independently by RNA polymerase II.

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Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain

Article Abstract:

A cotranscription event mediated by presence of capping enzyme with the RNA polymerase II phosphorylated carboxy-terminal domain (CTD) characterizes mRNA capping. In Saccharomyces cerevisiae yeast capping enzyme is made up of the mRNA 5'-triphosphatase (Cet1) and the mRNA guanylyltranferase (Ceg1). The guanylyltransferase subunit can bind by itself to the CTD, but cannot be guanylylated without the presence of the triphosphatase part. The yeast mRNA guanylyltransferease is regulated by allosteric interactions with the triphosphatase and the CTD. Interactions between Ceg1, Cet1, and the CTD are mapped

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