Small nucleolar RNA SNORD64

From WikiMD's Wellness Encyclopedia

Small nucleolar RNA SNORD64 (SNORD64), also known as U64, is a non-coding RNA (ncRNA) molecule which functions in the modification of other small nuclear RNAs (snRNAs). This type of modification is necessary for the maturation of pre-ribosomal RNA (rRNA) into mature rRNA, a key component of the ribosome. SNORD64 is a member of the C/D box class of snoRNAs which contain the conserved sequence motifs known as the C box (RUGAUGA) and the D box (CUGA). These molecules are involved in guiding the 2'-O-ribose methylation of rRNA molecules. SNORD64 is located within the introns of its host gene, which is a common characteristic of many snoRNAs.

Function[edit | edit source]

SNORD64 is involved in the biogenesis of the ribosome, the cellular structure responsible for protein synthesis. By guiding the 2'-O-methylation of specific residues on rRNA, SNORD64 plays a critical role in the structural and functional maturation of the ribosome. This modification process is essential for the accurate and efficient translation of mRNA into protein.

Biogenesis and Structure[edit | edit source]

Like other C/D box snoRNAs, SNORD64 is characterized by its conserved C and D boxes, which are crucial for its function in rRNA modification. The biogenesis of SNORD64 involves its transcription as part of a host gene, followed by processing to remove intronic sequences and form the mature snoRNA. The structure of SNORD64, like other snoRNAs, allows it to form complexes with specific proteins, forming small nucleolar ribonucleoproteins (snoRNPs). These complexes are essential for the snoRNA to perform its function in the nucleus.

Clinical Significance[edit | edit source]

While the specific clinical implications of SNORD64 have not been extensively characterized, dysregulation of snoRNAs, in general, has been associated with various diseases, including cancer. Abnormal expression levels of snoRNAs can affect ribosome biogenesis and function, potentially leading to altered protein synthesis and disease pathogenesis.

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Contributors: Prab R. Tumpati, MD