RNA-II and Elongator Complex: Potential Drug Targets and Biomarkers

Target Name: RNA polymerase II elongator complex

NCBI ID: P28636

RNA polymerase II elongator complex

Other Name(s): None

RNA-II and Elongator Complex: Potential Drug Targets and Biomarkers

RNA polymerase II (RNA-II) is a key enzyme in the process of transcription, where DNA is copied into RNA. RNA-II is composed of several subunits that work together to ensure the accuracy and efficiency of the transcription process. One of the subunits, called elongator complex, has been identified as a potential drug target or biomarker in several diseases.

The elongator complex is a subunit of RNA-II that is responsible for the extension of the 3' end of RNA chains. It is composed of the protein Elongator2 and the nucleotide-binding protein RNA-protein interaction domain (RISP). Elongator2 functions as a molecular scaffold, where it interacts with the template RNA and pulls the RNA chain along. RISP is a nucleotide-binding protein that recognizes the growing chain and releases a phosphate group, which can then be used to link in nucleotides to the growing RNA chain.

Studies have shown that dysregulation of RNA-II and elongator complex have been implicated in a number of diseases, including cancer, neurodegenerative diseases, and diseases associated with protein misfolding. In cancer, abnormal regulation of RNA-II and elongator complex have been observed to promote the growth and survival of cancer cells.

One of the potential drug targets for elongator complex is the inhibition of the enzyme heat shock protein (HSP) which is known to interact with elongator complex. HSPs are proteins that are produced in response to increased temperatures, and are involved in a variety of cellular processes, including DNA replication, protein folding, and stress response. By inhibiting HSPs, researchers have shown that they can reduce the activity of elongator complex and inhibit the growth and survival of cancer cells.

Another potential drug target for elongator complex is the targeting of the protein itself. Researchers have shown that blocking the activity of elongator complex can lead to the formation of protein-protein interfaces (PPIs) which can disrupt the structure and function of the complex. This disruptive effect has been observed to lead to the misfolding of proteins and the formation of aggregates, both of which can lead to the death of cells.

In addition to its potential as a drug target, elongator complex is also an attractive biomarker for several diseases. The elongation of RNA chains is a critical step in the transcription process, and the elongator complex is the only known protein that directly interacts with RNA- II. This means that changes in the activity of elongator complex have been observed to directly affect the amount of RNA produced from DNA.

Research has shown that changes in the elongator complex activity have been observed in a variety of diseases, including cancer, neurodegenerative diseases, and diseases associated with protein misfolding. For example, studies have shown that the elongator complex activity is increased in cancer cells and that inhibiting it has the potential to be an effective cancer therapeutic. Similarly, elongator complex has been shown to be involved in the development and progression of neurodegenerative diseases, and compounds that inhibit its activity have been shown to be effective in treating these diseases.

In conclusion, the elongator complex is a protein that plays a critical role in the transcription process and has been implicated in a number of diseases. Its activity is regulated by several factors, including HSPs and nucleotide-binding proteins. The elongator complex is an attractive drug target and a potential biomarker for several diseases, including cancer, neurodegenerative diseases, and diseases associated with protein misfolding. Further research is needed to fully understand its role in these diseases and to develop effective therapies that target it.

Protein Name: RNA Polymerase II Elongator Complex

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