invariantin

Invariantin is a protein that plays a crucial role in the regulation of the cell cycle and DNA repair. It was first identified in yeast and later found to be conserved across various eukaryotic organisms, including humans. The protein is characterized by its ability to bind to DNA and form complexes with other proteins, such as the DNA damage response proteins Rad53 and Rad51.

Invariantin's primary function is to facilitate the repair of DNA double-strand breaks (DSBs), which are a common type of DNA damage. It does this by recruiting the Rad51 recombinase to the site of damage, where it catalyzes the formation of a DNA strand invasion structure. This structure is then used as a template for the repair of the damaged DNA.

In addition to its role in DNA repair, invariantin has also been implicated in the regulation of the cell cycle. It has been shown to interact with the cyclin-dependent kinase Cdk1, which is a key regulator of the cell cycle. This interaction may play a role in the regulation of the transition from mitosis to interphase.

Invariantin is encoded by the INO80 gene in humans. Mutations in this gene have been associated with several genetic disorders, including Bloom syndrome and Werner syndrome. These disorders are characterized by an increased susceptibility to cancer and premature aging, respectively. The underlying mechanism of these disorders is thought to be related to the impaired DNA repair and cell cycle regulation functions of invariantin.

Overall, invariantin is a multifunctional protein that plays a critical role in maintaining genomic stability and regulating the cell cycle. Its functions are tightly regulated and coordinated with other proteins in the cell, ensuring the proper repair of DNA damage and the progression of the cell cycle.