PPM1G Human

Protein Phosphatase 1G (PP1G), also known as Protein Phosphatase 2C gamma (PP2C-gamma), is a member of the PP2C family of serine/threonine protein phosphatases. These phosphatases are known to be negative regulators of cell stress response pathways. PP1G plays a crucial role in various cellular processes, including the regulation of the cell cycle, apoptosis, and transcription.

Recombinant human PP1G is typically prepared using bacterial expression systems, such as Escherichia coli (E. coli). The gene encoding PP1G is cloned into an expression vector, which is then introduced into the bacterial cells. The bacteria are cultured, and the expression of the recombinant protein is induced. After sufficient expression, the bacterial cells are lysed, and the recombinant protein is purified using chromatography techniques. The purified protein often includes a His-tag at the N-terminus to facilitate purification and detection .

PP1G is involved in the dephosphorylation of pre-mRNA splicing factors, which is essential for the formation of functional spliceosomes. This dephosphorylation activity is crucial for the regulation of various cellular processes. The enzyme catalyzes the removal of phosphate groups from serine and threonine residues in target proteins, thereby modulating their activity. The catalytic activity of PP1G is dependent on the presence of divalent metal ions, such as magnesium or manganese .

The activity of PP1G is tightly regulated by various mechanisms. One of the primary regulatory mechanisms involves the interaction with specific regulatory subunits that target PP1G to particular subcellular locations. These regulatory subunits often contain conserved binding motifs that facilitate their interaction with PP1G. Additionally, the activity of PP1G can be modulated by post-translational modifications, such as phosphorylation and acetylation. These modifications can alter the enzyme’s conformation and, consequently, its activity .