Recombinant Human RRM1 protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RRM1 also known as ribonucleotide reductase large subunit or RNR1 plays an important role in DNA synthesis and repair converting ribonucleotides to deoxyribonucleotides. This enzyme has a mass of approximately 90 kDa. RRM1 is found in multiple tissues exhibiting especially high expression levels in proliferative tissues and tumors. Its activity is tightly regulated through the cell cycle and it is essential during DNA replication and cell division.

Biological function summary

The large subunit of ribonucleotide reductase contributes to the enzymatic function through binding and activation of smaller subunits including RRM2 and RRM2B forming a complex. This complex is important for maintaining balanced deoxyribonucleotide pools during the S-phase of the cell cycle. Proper RRM1 function ensures the fidelity of DNA synthesis impacting genomic stability and cell viability.

Pathways

RRM1 acts within the DNA replication and repair pathways. It interacts with the tumor suppressor protein p53 which modulates its activities in response to DNA damage. Through pathways like the p53-dependent checkpoint RRM1 contributes to DNA damage response mechanisms. This interaction with p53 and involvement in the DNA replication pathway highlight its centrality in maintaining genomic integrity.

RRM1 has connections with cancer and chemoresistance. Overexpression of RRM1 often correlates with increased tumor aggressiveness and poor prognosis in several cancers including lung and pancreatic cancers. In the context of chemoresistance RRM1 interplays with the excision repair cross-complementation group 1 protein (ERCC1) impacting the effectiveness of certain chemotherapies. Its role in these conditions makes it a target for cancer diagnosis and treatment strategies.