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Gene Review

NPL3  -  Npl3p

Saccharomyces cerevisiae S288c

Synonyms: D9461.19, MTR13, MTS1, Mitochondrial targeting suppressor 1 protein, NAB1, ...
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High impact information on NPL3

  • To ascertain the mechanism of this process, we show that RNA polymerase II transcription is sufficient to recruit the Saccharomyces cerevisiae hnRNP protein Npl3 to a gene independent of RNA sequence [1].
  • Combined mutations in the Saccharomyces cerevisiae hnRNP Npl3 and TATA-binding protein (TBP) block mRNA export, implying that cotranscriptional recruitment of Npl3 is required for efficient export of mRNA [2].
  • This import defect can be reversed by increasing the intracellular concentration of Mtr10p, the nuclear import receptor for Npl3p [3].
  • Interestingly, following induction of stress by heat shock, high salt, or ethanol, conditions under which most mRNA export is blocked, Npl3p is still exported from the nucleus [3].
  • Hmt1p methylates both Npl3p and Hrp1p, which are shuttling hnRNPs involved in mRNA processing and export [4].

Biological context of NPL3

  • HMT1 is not required for normal cell viability except when NPL3 is also defective [5].
  • Changes in the methylation status of Npl3p do not correlate with its nucleocytoplasmic distribution [6].
  • A crm1 mutant that inhibits export of proteins with leucine-rich nuclear export signals and mRNAs does not inhibit Npl3p export [6].
  • The discovery of two hnRNP homologues that can partially suppress the function of Npl3p, also an RNA binding protein, will be discussed in terms of the possible roles for Npl3p in RNA metabolism [7].
  • Our genetic analysis indicates that NPL3 is essential for normal cell growth; cells lacking NPL3 are temperature sensitive for growth but do not exhibit a defect in localization of nuclear proteins [8].

Anatomical context of NPL3


Associations of NPL3 with chemical compounds


Physical interactions of NPL3

  • However, cells missing HMT1 and also bearing mutations in the mRNA-binding proteins Npl3p or Cbp80p can no longer survive, providing genetic backgrounds in which to study Hmt1p function [16].
  • Purified Mtr10p forms a complex with Npl3p, an RNA-binding protein that shuttles in and out of the nucleus [17].

Enzymatic interactions of NPL3

  • Sky1p bound and phosphorylated Npl3 with a Km that was 2 orders of magnitude lower than a short peptide mimic representing the phosphorylation site and only proximal determinants [18].

Regulatory relationships of NPL3

  • Mutations in HRP1 suppress all npl3 temperature-sensitive alleles but do not bypass an npl3 null allele [7].
  • Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation [19].
  • These mutations also resulted in a decreased, methylation-independent interaction of Npl3 with transcription elongation factor Tho2 and inhibited Npl3 self-association [14].
  • We present evidence that the essential, nuclear phosphatase Glc7p promotes dephosphorylation of Npl3p in vivo and that nuclear dephosphorylation of Npl3p is required for mRNA export [20].

Other interactions of NPL3

  • The HRP1 gene was originally isolated as a suppressor of a temperature-sensitive npl3 allele, a gene encoding a protein involved in mRNA export [21].
  • Moreover, several proteins needed for Npl3p export are not needed for export of a typical Crm1p cargo [6].
  • We demonstrate that Npl3p is methylated by Hmt1p both in vivo and in vitro [5].
  • One of these is the previously known RNA15, which, like NPL3, also encodes a protein with similarity to the vertebrate hnRNP A/B protein family [7].
  • Roles of ABF1, NPL3, and YCL54 in silencing in Saccharomyces cerevisiae [22].
  • Npl3 competes with Rna15 for binding to a polyadenylation precursor and inhibits cleavage and polyadenylation in vitro [23].

Analytical, diagnostic and therapeutic context of NPL3


  1. Intron status and 3'-end formation control cotranscriptional export of mRNA. Lei, E.P., Silver, P.A. Genes Dev. (2002) [Pubmed]
  2. Messenger RNAs are recruited for nuclear export during transcription. Lei, E.P., Krebber, H., Silver, P.A. Genes Dev. (2001) [Pubmed]
  3. Uncoupling of the hnRNP Npl3p from mRNAs during the stress-induced block in mRNA export. Krebber, H., Taura, T., Lee, M.S., Silver, P.A. Genes Dev. (1999) [Pubmed]
  4. Arginine methylation facilitates the nuclear export of hnRNP proteins. Shen, E.C., Henry, M.F., Weiss, V.H., Valentini, S.R., Silver, P.A., Lee, M.S. Genes Dev. (1998) [Pubmed]
  5. A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins. Henry, M.F., Silver, P.A. Mol. Cell. Biol. (1996) [Pubmed]
  6. A Crm1p-independent nuclear export path for the mRNA-associated protein, Npl3p/Mtr13p. Liu, Y., Guo, W., Tartakoff, P.Y., Tartakoff, A.M. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  7. Potential RNA binding proteins in Saccharomyces cerevisiae identified as suppressors of temperature-sensitive mutations in NPL3. Henry, M., Borland, C.Z., Bossie, M., Silver, P.A. Genetics (1996) [Pubmed]
  8. A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast. Bossie, M.A., DeHoratius, C., Barcelo, G., Silver, P. Mol. Biol. Cell (1992) [Pubmed]
  9. A yeast protein that bidirectionally affects nucleocytoplasmic transport. Singleton, D.R., Chen, S., Hitomi, M., Kumagai, C., Tartakoff, A.M. J. Cell. Sci. (1995) [Pubmed]
  10. Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the translating mRNPs, and Npl3p can function as a translational repressor. Windgassen, M., Sturm, D., Cajigas, I.J., González, C.I., Seedorf, M., Bastians, H., Krebber, H. Mol. Cell. Biol. (2004) [Pubmed]
  11. NOP3 is an essential yeast protein which is required for pre-rRNA processing. Russell, I.D., Tollervey, D. J. Cell Biol. (1992) [Pubmed]
  12. Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. Yun, C.Y., Fu, X.D. J. Cell Biol. (2000) [Pubmed]
  13. 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]
  14. Arginine methylation of yeast mRNA-binding protein Npl3 directly affects its function, nuclear export, and intranuclear protein interactions. McBride, A.E., Cook, J.T., Stemmler, E.A., Rutledge, K.L., McGrath, K.A., Rubens, J.A. J. Biol. Chem. (2005) [Pubmed]
  15. Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins. Häcker, S., Krebber, H. J. Biol. Chem. (2004) [Pubmed]
  16. Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. McBride, A.E., Weiss, V.H., Kim, H.K., Hogle, J.M., Silver, P.A. J. Biol. Chem. (2000) [Pubmed]
  17. Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. Senger, B., Simos, G., Bischoff, F.R., Podtelejnikov, A., Mann, M., Hurt, E. EMBO J. (1998) [Pubmed]
  18. Chemical clamping allows for efficient phosphorylation of the RNA carrier protein Npl3. Aubol, B.E., Ungs, L., Lukasiewicz, R., Ghosh, G., Adams, J.A. J. Biol. Chem. (2004) [Pubmed]
  19. Phosphorylation by Sky1p promotes Npl3p shuttling and mRNA dissociation. Gilbert, W., Siebel, C.W., Guthrie, C. RNA (2001) [Pubmed]
  20. The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA. Gilbert, W., Guthrie, C. Mol. Cell (2004) [Pubmed]
  21. Hrp1, a sequence-specific RNA-binding protein that shuttles between the nucleus and the cytoplasm, is required for mRNA 3'-end formation in yeast. Kessler, M.M., Henry, M.F., Shen, E., Zhao, J., Gross, S., Silver, P.A., Moore, C.L. Genes Dev. (1997) [Pubmed]
  22. Roles of ABF1, NPL3, and YCL54 in silencing in Saccharomyces cerevisiae. Loo, S., Laurenson, P., Foss, M., Dillin, A., Rine, J. Genetics (1995) [Pubmed]
  23. Polyadenylation site choice in yeast is affected by competition between Npl3 and polyadenylation factor CFI. Bucheli, M.E., He, X., Kaplan, C.D., Moore, C.L., Buratowski, S. RNA (2007) [Pubmed]
  24. 7The yeast mRNA-binding protein Npl3p interacts with the cap-binding complex. Shen, E.C., Stage-Zimmermann, T., Chui, P., Silver, P.A. J. Biol. Chem. (2000) [Pubmed]
  25. Yeast Nop3p has structural and functional similarities to mammalian pre-mRNA binding proteins. Russell, I., Tollervey, D. Eur. J. Cell Biol. (1995) [Pubmed]
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