High impact information on NOP5/NOP58

• In contrast, as shown previously, stem II of the kink-turn motif in box C/D snoRNAs is comprised of three base pairs, and NOP56 and NOP58 require a G-C pair at the central position [1].
• Structural and thermodynamic evidence for a stabilizing role of Nop5p in S-adenosyl-L-methionine binding to fibrillarin [2].
• This structure exhibited a pre-formed backbone geometry at the cofactor binding site similar to that when the cofactor is bound, suggesting that binding of Nop5p alone to fibrillarin is sufficient to stabilize the AdoMet-binding pocket [2].
• Our results suggest that L7Ae facilitates the folding of the K-turn motifs (chaperone function) and, in addition, is required for methylation activity in the presence of Nop5 and Fib [3].
• Human NOP5 cDNA was isolated from an M426 fibroblast cDNA library [4].

Biological context of NOP5/NOP58

• In Archaea, fibrillarin and Nop5p form the core complex of box C/D small ribonucleoprotein particles, which are responsible for site-specific 2'-hydroxyl methylation of ribosomal and transfer RNAs [2].

Associations of NOP5/NOP58 with chemical compounds

• Pretreatment with cycloheximide enhanced, while actinomycin blocked induction of the NOP5 transcript [4].

Other interactions of NOP5/NOP58

• To identify the structural elements responsible for these large conformational differences, we refined a crystal structure of Archaeoglobus fulgidus fibrillarin-Nop5p binary complex at 3.5 A [2].

Analytical, diagnostic and therapeutic context of NOP5/NOP58

• Ubiquitous, but differential NOP5 mRNA expression was revealed after Northern blot analysis of total RNA from several human tissues [4].
• Using a differential display RT-PCR strategy to identify novel growth-factor-induced transcripts, we cloned and characterized the human homolog of yeast NOP5/NOP58, whose gene product has been implicated in the execution of early pre-rRNA processing steps [4].

References