60S ribosomal protein L18a

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60S ribosomal protein L18a is a protein that in humans is encoded by the RPL18A gene. This protein is a component of the 60S ribosomal subunit which is part of the ribosome, the cell's molecular machine for protein synthesis. Ribosomal proteins play a key role in the function of the ribosome, facilitating the assembly of the ribosomal subunits and ensuring the proper translation of mRNA into protein.

Function[edit | edit source]

The 60S ribosomal protein L18a is involved in the assembly and structural stability of the 60S ribosomal subunit. It interacts with RNA and other ribosomal proteins to form the ribosome, where amino acids are linked together to form proteins, a process essential for cell growth and division. This protein is one of the larger components of the ribosome and contributes to the formation of the peptidyl transferase center, where peptide bonds are formed between amino acids.

Gene[edit | edit source]

The RPL18A gene is located on the chromosome 5 in humans. It contains the instructions for synthesizing the 60S ribosomal protein L18a. Like other ribosomal protein genes, RPL18A is expressed in all cell types, reflecting the essential role of ribosomes in all cellular functions.

Clinical Significance[edit | edit source]

Alterations in the expression or function of ribosomal proteins, including 60S ribosomal protein L18a, can lead to diseases known as ribosomopathies. These are a group of disorders arising from defects in ribosomal function, which can result in a variety of clinical manifestations including developmental abnormalities and increased susceptibility to cancer. However, specific diseases associated directly with mutations in the RPL18A gene have not been well-characterized.

Evolution[edit | edit source]

Ribosomal proteins are highly conserved throughout evolution, indicating their fundamental role in the biology of all living organisms. The 60S ribosomal protein L18a shares a high degree of similarity across different species, from yeast to humans, underscoring its essential function in the ribosome.

See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD