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Gene Review:

SNORA75 - small nucleolar RNA, H/ACA box 75

Homo sapiens

Synonyms: U23

Steenkamp, D.J. et al., Brodsky, A.S. et al., Jawis, M.N. et al., Puglisi, J.D. et al., Churcher, M.J. et al., et al.

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High impact information on SNORA75

Upon arginine binding, the bulge changes conformation, and essential nucleotides for binding, U23 and A27.U38, form a base-triple interaction that stabilizes arginine hydrogen bonding to G26 and phosphates [1].
Argininamide binding is stabilized by stacking of the guanidinium group between the bases of A22 and U23, forming an argininamide sandwich [2].
As observed in the previously proposed model from this lab, the two A-form stems co-axially stack and the critical U23 and the argininamide are located in the major groove [2].
Mutations in U23, a critical residue in the U-rich "bulge" sequence, or in either of the two base-pairs immediately above the "bulge", G26.C39 and A27.U38 reduced that affinity by 8- to 20-fold [3].
The results indicated identity of U23 with 1-N-methyl-4-mercaptohistidine (ovothiol A), previously isolated from marine sources [4].

Biological context of SNORA75

The distal evolutionary breakpoint on human chromosome 12, producing the chromosomal segment U23 in cattle marked by aldehyde dehydrogenase (ALDH2), also produces a separate segment in sheep [5].
Mean maximum heart rate during exercise was significantly higher in the U15 group when compared to the U18 and U23 groups (p<0.05) [6].

Anatomical context of SNORA75

RESULTS: The U23 players were significantly taller and heavier with significantly better ROM of the neck, trunk, and ankle joints and back and leg strength than the U15 players [6].

Associations of SNORA75 with chemical compounds

U23 and G26 are brought into close proximity by contacts to the guanidinium group and side-chain amide group of a common arginine residue [7].
Resonances attributable to U23 were discerned from those of the bimane label by comparison of the 1H- and 13C-NMR spectra of monobromobimane and U23-bimane [4].

Analytical, diagnostic and therapeutic context of SNORA75

This assignment was confirmed by NOE difference experiments, fast-atom-bombardment mass spectrometry of U23-bimane and ultraviolet/visible spectrophotometry of U23, which was isolated as the disulfide [4].

References

Conformation of the TAR RNA-arginine complex by NMR spectroscopy. Puglisi, J.D., Tan, R., Calnan, B.J., Frankel, A.D., Williamson, J.R. Science (1992) [Pubmed]
Solution structure of the HIV-2 TAR-argininamide complex. Brodsky, A.S., Williamson, J.R. J. Mol. Biol. (1997) [Pubmed]
High affinity binding of TAR RNA by the human immunodeficiency virus type-1 tat protein requires base-pairs in the RNA stem and amino acid residues flanking the basic region. Churcher, M.J., Lamont, C., Hamy, F., Dingwall, C., Green, S.M., Lowe, A.D., Butler, J.G., Gait, M.J., Karn, J. J. Mol. Biol. (1993) [Pubmed]
Identification of a major low-molecular-mass thiol of the trypanosomatid Crithidia fasciculata as ovothiol A. Facile isolation and structural analysis of the bimane derivative. Steenkamp, D.J., Spies, H.S. Eur. J. Biochem. (1994) [Pubmed]
Mapping of MYF5, C1R, MYHL, TPI1, IAPP, A2MR and RNR onto sheep chromosome 3q. Broad, T.E., Burkin, D.J., Jones, C., Lewis, P.E., Ansari, H.A., Pearce, P.D. Anim. Genet. (1993) [Pubmed]
Anthropometric and physiological profiles of sepak takraw players. Jawis, M.N., Singh, R., Singh, H.J., Yassin, M.N. British journal of sports medicine. (2005) [Pubmed]
The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein. Aboul-ela, F., Karn, J., Varani, G. J. Mol. Biol. (1995) [Pubmed]

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