RNA Polymerase II and Psoriasis

Title: RNA Polymerase II subunit 3 is retained in the cytoplasm by its interaction with HCR, the psoriasis vulgaris candidate gene product.
: Corbi N, et al.
Publication: J Cell Sci. 2005 Sep 15;118(Pt 18):4253-4260. Epub 2005 Sep 1.

The authors have recently demonstrated that the expression of alpha-like RNA polymerase II core subunit 3 (RPB3) was regulated during the differentiation or formation of muscle cells. RPB3 was also found inside RNA polymerase II (RNAP II), and was directly involved in contacting regulatory proteins.

In this article, the authors showed that RPB3 molecules accumulated in the cytoplasm of cycling myogenic cells or muscle cells that still undergo cell cycles or cellular division. Upon differentiation or formation of muscle cells, RPB3 migrated to the cell nucleus.

Using a technique called yeast two-hybrid system, the authors identified a novel RPB3 cytoplasmic interacting protein called HCR. HCR was previously identified as alpha-helix coiled-coil rod homologue, and is one of the candidate genes for psoriasis vulgaris.

The authors showed that in cycling muscle cells, the RPB3 protein interact directly with HCR within the cytoplasm. When they reduced the HCR level, the authors demonstrated that the protein act as a docking site for RPB3 in the cytoplasm.

Editor’s Note: RNA polymerase II is a protein that creates mRNA (messenger RNA) from the DNA sequence of a particular gene. The mRNA copy is then used to make proteins.

The yeast two-hybrid system is a widely used technique used to identify proteins that that bind or interact with each other. The authors artificially reduced the HCR level by using RNA interference, where the presence of a double-stranded RNA interferes with the expression of a particular gene.

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