GLC8 Yeast

The recombinant GLC8 protein is typically produced in Escherichia coli and is fused with a His-tag at the N-terminus for purification purposes. The protein consists of 229 amino acids and has a molecular weight of approximately 30.7 kDa . The amino acid sequence of the recombinant GLC8 protein includes several regions that are crucial for its regulatory functions.

GLC8 is involved in several key biological processes:

1. Glycogen Metabolism: GLC8 regulates the activity of Glc7p, which is essential for glycogen biosynthesis. This regulation ensures proper glycogen storage and mobilization within the cell .
2. Chromosome Segregation: GLC8 plays a role in chromosome segregation during cell division. It helps maintain the fidelity of chromosome distribution to daughter cells .
3. Response to DNA Replication Stress: The abundance of GLC8 protein increases in response to DNA replication stress, indicating its role in the cellular stress response .

Under normal conditions, GLC8 activates Glc7p. However, when GLC8 is overproduced, it may inhibit Glc7p function. This dual role is mediated through phosphorylation by the Pho85p complexed with cyclins such as Pcl6p, Pcl7p, Pcl8p, or Pcl10p .

Recombinant GLC8 protein is used in various research applications, including studies on glycogen metabolism, cell cycle regulation, and stress response mechanisms. It is also utilized in biochemical assays to understand the regulatory mechanisms of protein phosphatases.

The recombinant GLC8 protein should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain protein integrity. The protein is typically supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, and 10% glycerol .