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Gene Review

NHP2  -  snoRNA-binding protein NHP2

Saccharomyces cerevisiae S288c

Synonyms: D1045, H/ACA ribonucleoprotein complex subunit 2, H/ACA snoRNP protein NHP2, High mobility group-like nuclear protein 2, YDL208W
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High impact information on NHP2

  • Using the snR81-deletion strain, Nhp2p- or Cbf5p-conditional depletion strain, and a cbf5 mutation strain, we further demonstrated that the pseudouridylase activity is dependent on snR81 snoRNP in vivo [1].
  • Surprisingly, we found a Psi42-specific pseudouridylase activity that coincided with Nhp2p, a protein component of a Box H/ACA sno/scaRNP (small nucleolar/Cajal body-specific ribonucleoprotein) [1].
  • These phenotypes are probably a direct consequence of the instability of H/ACA snoRNAs and Gar1p observed in cells deprived of Nhp2p or Nop10p [2].
  • We report the identification of a novel nucleolar protein from fission yeast, p17(nhp2), which is homologous to the recently identified Nhp2p core component of H+ACA snoRNPs in Saccharomyces cerevisiae [3].
  • Functional conservation and cell cycle localization of the Nhp2 core component of H + ACA snoRNPs in fission and budding yeasts [3].

Biological context of NHP2

  • However, nucleotide sequence analysis revealed that NHP2 could encode a 17.1 kilodalton basic protein which was not significantly homologous to any previously sequenced HMG proteins [4].
  • A search of protein databases showed that the amino acid sequence of NHP2 shared significant identities with two ribosomal proteins; the acidic ribosomal protein S6 from Halobacterium marismorium and protein L7a from mammals [4].
  • Finally, NHP2 has been shown to have a critical role in the cell; when a diploid yeast strain deleted of one copy of the NHP2 gene was sporulated and dissected, only half of the spores grew into normal colonies [4].
  • We have isolated a novel human cDNA that encodes a protein highly homologous to NHP2, a nuclear protein of yeast, that is thought to have an essential physiological function for cell viability [5].

Anatomical context of NHP2

  • NHP2 has been called 'HMG-like' because of the physical/chemical properties it shares with the HMG proteins from higher eukaryotic cells [4].

Associations of NHP2 with chemical compounds

  • Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs [6].
  • Glycerol gradient sedimentation and sequential immunoprecipitation experiments suggest that the Lsm protein-snR5 complex is partly distinct from the complex formed by snR5 RNA with the box H/ACA proteins Gar1p and Nhp2p [7].
  • The sequence of p54 is 60% identical with that of the precursor of a sucrose-binding soybean protein, and, to a lesser extent (31-34%), it shares homology with some storage proteins. p16 is also 30% homologous with Nhp2p, a yeast nuclear protein [8].

Other interactions of NHP2


Analytical, diagnostic and therapeutic context of NHP2

  • To address this problem and further complete the snoRNA assignment to Psi sites, we identified the complete set of RNAs associated with the H/ACA snoRNP specific proteins Gar1p and Nhp2p by coupling TAP-tag purifications with genomic DNA microarrays experiments [10].
  • Sequence analysis of the individual polypeptides demonstrated that the three proteins Gar1p, Nhp2p, and Cbf5p are common to both the snR30 and snR42 complexes [11].


  1. Pseudouridylation of yeast U2 snRNA is catalyzed by either an RNA-guided or RNA-independent mechanism. Ma, X., Yang, C., Alexandrov, A., Grayhack, E.J., Behm-Ansmant, I., Yu, Y.T. EMBO J. (2005) [Pubmed]
  2. Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs. Henras, A., Henry, Y., Bousquet-Antonelli, C., Noaillac-Depeyre, J., Gélugne, J.P., Caizergues-Ferrer, M. EMBO J. (1998) [Pubmed]
  3. Functional conservation and cell cycle localization of the Nhp2 core component of H + ACA snoRNPs in fission and budding yeasts. Maiorano, D., Brimage, L.J., Leroy, D., Kearsey, S.E. Exp. Cell Res. (1999) [Pubmed]
  4. Sequence and genetic analysis of NHP2: a moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae. Kolodrubetz, D., Burgum, A. Yeast (1991) [Pubmed]
  5. Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a protein highly homologous to yeast nuclear protein NHP2. Saito, H., Fujiwara, T., Shin, S., Okui, K., Nakamura, Y. Cytogenet. Cell Genet. (1996) [Pubmed]
  6. Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs. Henras, A.K., Capeyrou, R., Henry, Y., Caizergues-Ferrer, M. RNA (2004) [Pubmed]
  7. An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5. Fernandez, C.F., Pannone, B.K., Chen, X., Fuchs, G., Wolin, S.L. Mol. Biol. Cell (2004) [Pubmed]
  8. A pea nuclear protein that is induced by dehydration belongs to the vicilin superfamily. Castillo, J., Rodrigo, M.I., Márquez, J.A., Zúñiga, A., Franco, L. Eur. J. Biochem. (2000) [Pubmed]
  9. Naf1 p is a box H/ACA snoRNP assembly factor. Fatica, A., Dlakić, M., Tollervey, D. RNA (2002) [Pubmed]
  10. The complete set of H/ACA snoRNAs that guide rRNA pseudouridylations in Saccharomyces cerevisiae. Torchet, C., Badis, G., Devaux, F., Costanzo, G., Werner, M., Jacquier, A. RNA (2005) [Pubmed]
  11. Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure. Watkins, N.J., Gottschalk, A., Neubauer, G., Kastner, B., Fabrizio, P., Mann, M., Lührmann, R. RNA (1998) [Pubmed]
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