60S ribosomal protein L23a

60S ribosomal protein L23a is a protein that in humans is encoded by the RPL23A gene. This protein is a component of the 60S subunit of the ribosome, playing a critical role in protein synthesis. Ribosomes, the cellular machines responsible for making proteins, are composed of two subunits, the 40S (small subunit) and the 60S (large subunit), each of which contains its own set of proteins and ribosomal RNA (rRNA). The 60S ribosomal protein L23a is integral to the function of the 60S subunit in the eukaryotic ribosome.

Function

The primary function of 60S ribosomal protein L23a is to contribute to the structural stability of the ribosome and facilitate the correct positioning of the rRNA and other ribosomal proteins within the 60S subunit. This positioning is crucial for the ribosome's ability to translate messenger RNA (mRNA) sequences into proteins. Specifically, L23a is thought to play a role in the peptidyl transferase center of the ribosome, where peptide bonds are formed between amino acids to elongate a growing protein chain. Additionally, L23a is involved in the export of the 60S subunit from the nucleus to the cytoplasm, a critical step in ribosome assembly.

Gene

The RPL23A gene is located on chromosome 17 in humans. It encodes the 60S ribosomal protein L23a, which is highly conserved across eukaryotes, indicating its essential role in the ribosome's function. The gene's conservation across different species underscores the fundamental and universal mechanism of protein synthesis in living organisms.

Clinical Significance

Alterations in the expression of the RPL23A gene have been associated with various forms of cancer. Overexpression of 60S ribosomal protein L23a has been observed in some tumors, suggesting a potential role in tumorigenesis. This association is believed to be due to the protein's involvement in cellular growth and proliferation, processes that are often dysregulated in cancer cells. However, the exact mechanism by which L23a contributes to cancer development remains an area of ongoing research.

See Also

• Ribosome
• Protein synthesis
• Ribosomal proteins