A protein phosphatase functions to recycle RNA polymerase II

Article Abstract:

A protein phosphatase recycles RNA polymerase II, based on work in which a cDNA clone that encodes a 15-kD polypeptide, which reconstitutes a very specific carboxy-terminal domain (CTD) phosphatase activity, was isolated. The reconstitution takes place with the polypeptide working with RNA polymerase II (RNAPII, the CTD phosphatase). The phosphatase stimulates elongation by RNAPII, but independent of phosphatase catalysis. The CTD phosphatase is active in ternary elongation complexes.

Phosphorylation, Phosphatases

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SNAP(sub.c): a core promoter factor with a built-in DNA-binding damper that is deactivated by the Oct-1 POU domain

Article Abstract:

SNAP(sub.c), that is, snRNA activating protein complex, a core promoter factor with a built-in DNA-binding damper that the Oct-1 POU domain deactivates, is discussed. The roles of SNAP(sub.c) components, of which there are five, have been determined in some processes it is known to be involved in by putting parts of it together in vitro.

Protein binding

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Transcription elongation factor hSPT5 stimulates mRNA capping

Article Abstract:

Stimulation of mRNA capping by transcription elongation factor hSPT5, the human homolog of yeast elongation factor SPT5, is discussed based on recent research. TFIIH-phosphorylated CRD stimulates guanylylation in an increase not additive with hSPT5, and hSPT5 did not increase activity of the guanylyltransferase fragment.

Cellular control mechanisms, Cell regulation

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