60S ribosomal protein L34
60S ribosomal protein L34 is a protein that in humans is encoded by the RPL34 gene. This protein is a component of the 60S ribosomal subunit, which is part of the larger ribosome complex responsible for protein synthesis within the cell. The 60S subunit works in conjunction with the 40S ribosomal subunit to translate messenger RNA (mRNA) sequences into polypeptide chains, which then fold into functional proteins.
Function[edit | edit source]
The 60S ribosomal protein L34, like other ribosomal proteins, plays a critical role in the process of translation, the step in gene expression where the ribosome decodes mRNA into a protein. Specifically, it is involved in the assembly and structural stability of the 60S ribosomal subunit. Proteins in the ribosomal subunit are essential for accurate and efficient protein synthesis. They ensure the proper alignment of mRNA and transfer RNA (tRNA), and facilitate the catalytic steps of peptide bond formation.
Gene[edit | edit source]
The RPL34 gene is located on chromosome 1 in humans. It encodes the 60S ribosomal protein L34, which is highly conserved across different species, indicating its essential role in the ribosome's function. The gene's conservation across species underscores the fundamental and universal mechanism of protein synthesis in eukaryotes.
Clinical Significance[edit | edit source]
Alterations in ribosomal proteins, including 60S ribosomal protein L34, can lead to various diseases, known collectively as ribosomopathies. These conditions are characterized by defects in ribosome function and assembly, leading to widespread cellular dysfunction. While specific mutations in the RPL34 gene have not been extensively characterized in the context of human disease, disruptions in ribosomal protein genes can contribute to disorders such as Diamond-Blackfan anemia and certain forms of cancer. Research into ribosomal proteins and their genes continues to provide insights into the complex relationship between ribosome function and human disease.
See Also[edit | edit source]
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