Recombinant Human MRPS25 protein (denatured)

Supplementary information

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

MRPS25 also known as Mitochondrial Ribosomal Protein S25 is a component of the mitochondrial ribosome. It has a molecular mass of approximately 17.92 kDa. MRPS25 is expressed in various tissues with notable expression in mitochondria-rich tissues like the heart and skeletal muscle. Its role as part of the small 28S subunit of the mitochondrial ribosome highlights its importance in mitochondrial protein synthesis facilitating the creation of proteins encoded by mitochondrial DNA.

Biological function summary

MRPS25 contributes to the synthesis of proteins important for mitochondrial function. The protein plays a role in assembling the mitochondrial ribosome complex where it works alongside other ribosomal proteins and mitochondrial rRNA. This protein by being part of the mitochondrial ribosome helps maintain the balance of mitochondrial protein content ensuring effective cellular respiration and energy production in cells with high metabolic demands.

Pathways

MRPS25's involvement in mitochondrial translation is significant. It is an important participant in the OXPHOS (oxidative phosphorylation) pathway essential for ATP production. In this context it interacts with other mitochondrial ribosomal proteins such as MRPS2 and MRPS5. By supporting mitochondrial protein synthesis MRPS25 indirectly affects various metabolic pathways that rely on mitochondrial energy production and maintenance.

MRPS25 links to mitochondrial disorders and conditions impacting energy metabolism. Mutations or dysfunction in MRPS25 may contribute to mitochondrial diseases characterized by reduced ATP production and energy deficits. In some cases these changes may relate to neuromuscular disorders where efficient mitochondrial function is necessary. Proteins like MRPS5 which co-exist in the mitochondrial ribosome may exhibit changes alongside MRPS25 in the context of such disorders further compromising mitochondrial function.