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Gene Review

NSR1  -  Nsr1p

Saccharomyces cerevisiae S288c

Synonyms: G7001, Nuclear localization sequence-binding protein, YGR159C, p67
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High impact information on NSR1

  • The NH2-terminal domain of Fpr3 contains long stretches of acidic residues alternating with blocks of basic residues, a structure that resembles sequences found in nucleolar proteins, including S. cerevisiae NSR1 and mammalian nucleolin [1].
  • NSR1 has three regions: an acidic/serine-rich NH2 terminus, two RNA recognition motifs, and a glycine/arginine-rich COOH terminus [2].
  • Interestingly, the NSR1 protein has two RNA recognition motifs, as well as an acidic NH2 terminus containing a series of serine clusters, and a basic COOH terminus containing arg-gly repeats [3].
  • We have also shown that NSR1 (p67) is required for normal cell growth [3].
  • We report here the isolation and characterization of the nucMs1 alfalfa cDNA, whose predicted amino acid sequence structurally resembles the yeast Nsr1 protein and animal nucleolins [4].

Biological context of NSR1

  • NSR1, a 67-kD nucleolar protein, was originally identified in our laboratory as a nuclear localization signal binding protein, and has subsequently been found to be involved in ribosome biogenesis [2].
  • The yeast nucleolar protein-encoding gene NSR1 was isolated by low-stringency screening of a yeast genomic library with the human heterogeneous nuclear ribonucleoprotein type A1 (hnRNP A1) cDNA probe, and was mapped to chromosome VII [5].
  • The carboxyl-terminal half of NSR1, consisting of two tandemly repeated putative RNA-binding domains and a glycine/arginine-rich domain, has 37% amino acid sequence identity with the same part of mammalian nucleolin, while no sequence similarities are found between their amino-terminal regions [6].
  • We report here the regulation of NSR1 gene expression and the effect of nsr1 deletion on growth and pre-rRNA processing after cold shock [7].
  • Developmental and cell cycle regulation of alfalfa nucMs1, a plant homolog of the yeast Nsr1 and mammalian nucleolin [4].

Anatomical context of NSR1


Associations of NSR1 with chemical compounds

  • Among the few proteins of the eukaryotic nucleolus that have been characterized, four proteins, nucleolin, fibrillarin, SSB1 and NSR1, possess a common structural motif, the GAR domain, which is rich in glycine and arginine residues [9].
  • Yeast strains carrying a deletion of the NSR1 gene have a defect in rRNA processing, an aberrant ribosome profile and are sensitive to the drug paromomycin [10].
  • A comparison between the Nsr1 and hnRNP A1 proteins, based on homopolymer RNA binding to their structural domains in vitro, revealed a striking biochemical similarity [5].
  • The 67 amino acid carboxyl-terminal domain (P67) of human propionyl-CoA carboxylase alpha subunit can be metabolically biotinylated at a fixed lysine residue [11].

Physical interactions of NSR1

  • Our findings are consistent with the notion that nucleolar localization is a result of the binding interactions of various domains of NSR1 within the nucleolus rather than the presence of a specific nucleolar targeting signal [2].

Other interactions of NSR1


Analytical, diagnostic and therapeutic context of NSR1

  • These results suggest that when combined with P67-based biotinylation, anti-TfR IgG3-Av could serve as a universal delivery vector for targeted chemotherapy of cancer [11].


  1. A novel FK506- and rapamycin-binding protein (FPR3 gene product) in the yeast Saccharomyces cerevisiae is a proline rotamase localized to the nucleolus. Benton, B.M., Zang, J.H., Thorner, J. J. Cell Biol. (1994) [Pubmed]
  2. Multiple regions of NSR1 are sufficient for accumulation of a fusion protein within the nucleolus. Yan, C., Mélèse, T. J. Cell Biol. (1993) [Pubmed]
  3. The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. Lee, W.C., Xue, Z.X., Mélèse, T. J. Cell Biol. (1991) [Pubmed]
  4. Developmental and cell cycle regulation of alfalfa nucMs1, a plant homolog of the yeast Nsr1 and mammalian nucleolin. Bögre, L., Jonak, C., Mink, M., Meskiene, I., Traas, J., Ha, D.T., Swoboda, I., Plank, C., Wagner, E., Heberle-Bors, E., Hirt, H. Plant Cell (1996) [Pubmed]
  5. Analysis of the yeast NSR1 gene and protein domain comparison between Nsr1 and human hnRNP type A1. Gamberi, C., Contreas, G., Romanelli, M.G., Morandi, C. Gene (1994) [Pubmed]
  6. Yeast NSR1 protein that has structural similarity to mammalian nucleolin is involved in pre-rRNA processing. Kondo, K., Inouye, M. J. Biol. Chem. (1992) [Pubmed]
  7. Cold shock induction of yeast NSR1 protein and its role in pre-rRNA processing. Kondo, K., Kowalski, L.R., Inouye, M. J. Biol. Chem. (1992) [Pubmed]
  8. Identification and characterization of a nuclear localization sequence-binding protein in yeast. Lee, W.C., Mélèse, T. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  9. GAR1 is an essential small nucleolar RNP protein required for pre-rRNA processing in yeast. Girard, J.P., Lehtonen, H., Caizergues-Ferrer, M., Amalric, F., Tollervey, D., Lapeyre, B. EMBO J. (1992) [Pubmed]
  10. Inheritance of suppressors of the drug sensitivity of a NSR1 deleted yeast strain. Zabetakis, D. Yeast (2000) [Pubmed]
  11. A human biotin acceptor domain allows site-specific conjugation of an enzyme to an antibody-avidin fusion protein for targeted drug delivery. Asai, T., Trinh, R., Ng, P.P., Penichet, M.L., Wims, L.A., Morrison, S.L. Biomol. Eng. (2005) [Pubmed]
  12. In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p. Xu, C., Henry, P.A., Setya, A., Henry, M.F. RNA (2003) [Pubmed]
  13. Construction of a GAL1-regulated yeast cDNA expression library and its application to the identification of genes whose overexpression causes lethality in yeast. Liu, H., Krizek, J., Bretscher, A. Genetics (1992) [Pubmed]
  14. Isolation and characterization of two Saccharomyces cerevisiae genes that encode proteins that bind to (TG1-3)n single strand telomeric DNA in vitro. Lin, J.J., Zakian, V.A. Nucleic Acids Res. (1994) [Pubmed]
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