RNA polymerase II is a large 12-subunit complex that synthesizes all mRNAs and several non-coding RNAs in eukaryotic cells. It is a DNA-dependent RNA polymerase enzyme that catalyzes transcription of DNA into RNA based on the four ribonucleoside triphosphate building blocks. RNA polymerase II is regulated through DNA-binding transcriptional regulators in both gene and cell type-specific manners. General transcription factors act as RNA polymerase II accessory proteins for transcription of most class II genes, while co-activators and co-repressors bridge between DNA-bound factors and the transcription machinery. The largest subunit B1 is also the catalytic component that forms the active center along with the second largest subunit. The complex is composed of mobile elements surrounding a large central cleft that open and closes due to a flexible clamp. RNAPII antibody was used in a yeast reconstituted system to demonstrate that the DEF1 gene is required for RNAPII ubiquitination, and that this mechanism is DNA damage-dependent1. In deep sequencing studies done by Cheng’s group, they used a panel of antibodies that included an RNAPII antibody to identify a unique cytoplasmic membrane-associated transcription system that is chemically different from its nuclear counterpart2.
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Immunocytochemistry/Immunofluorescence: RNA polymerase II Antibody
RNAPII antibody allowed Hamasaki, et al. to characterize the novel HIV-1 inhibitors C1, C2, and C3 and determine their mechanism to be CycT1/Tat-mediated3. By using the RNAPII antibody, Walsh’s group was able to adopt a multidimensional proteomics approach in their CHiP studies on transcription factor occupancy of the luteinizing hormone (LH) beta-subunit promoter4. This group found that proteasomal degradation is vital to LH expression in response to GnRH. The RNAPII antibody as also used in CHiP studies in a fission yeast system where investigators were studying the storage of epigenetic information in the a posttranslationally modified histone H3 compartment5.
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