60S ribosomal protein L28

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Ideogram human chromosome 19.svg

60S ribosomal protein L28 is a protein that in humans is encoded by the RPL28 gene. This protein is a component of the 60S subunit of the ribosome, playing a critical role in the protein synthesis process. Ribosomes, consisting of two subunits, 40S and 60S, are essential for the translation of mRNA into protein. The 60S ribosomal protein L28 is one of the many proteins that make up the larger 60S subunit and is involved in the assembly and structural stability of the ribosome.

Function[edit | edit source]

The primary function of the 60S ribosomal protein L28 is to contribute to the structural integrity and function of the ribosome's 60S subunit. It participates in the assembly of the ribosome and plays a role in the binding of tRNA and mRNA molecules, facilitating the accurate translation of mRNA into a polypeptide chain. Proteins like RPL28 are crucial for the ribosome's ability to synthesize proteins efficiently and accurately.

Gene[edit | edit source]

The RPL28 gene is located on chromosome 19 in humans and contains the genetic information necessary to produce the 60S ribosomal protein L28. The expression of this gene, like many ribosomal protein genes, is tightly regulated to meet the cell's demands for protein synthesis.

Clinical Significance[edit | edit source]

Alterations in the expression or function of ribosomal proteins, including RPL28, can lead to various diseases, known as ribosomopathies. These conditions often result from impaired ribosome biogenesis or function, leading to specific cellular and physiological defects. However, the direct involvement of RPL28 in specific diseases has not been extensively characterized, making it an area of ongoing research.

Evolution[edit | edit source]

Ribosomal proteins are highly conserved throughout evolution, indicating their fundamental role in the biology of all living organisms. The conservation of proteins like RPL28 across different species underscores the essential, universal mechanisms of protein synthesis.

See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD