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NUP49  -  Nup49p

Saccharomyces cerevisiae S288c

Synonyms: G1648, NSP49, Nuclear pore protein NUP49/NSP49, Nucleoporin NUP49/NSP49, YGL172W
 
 
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High impact information on NUP49

  • We show that a pool of green fluorescent protein-tagged Sec13p localizes to the nuclear pores in vivo, and identify sec13 mutant alleles that are synthetically lethal with nup85Delta and affect the localization of a green fluorescent protein-Nup49p reporter protein [1].
  • However, thermosensitive rna1-1 (Ran-GAP), prp20-1 (Ran-GEF), and nucleoporin nup49 and nsp1 mutants are impaired in ribosomal export as revealed by nuclear accumulation of L25-GFP [2].
  • Indirect immunofluorescence microscopy shows that Ndc1p displays punctate, nuclear peripheral localization that colocalizes with a known NPC component, Nup49p [3].
  • Under these conditions, the use of GFP-Nup133p and GFP-Nup49p fusion proteins revealed that Nup133p can be rapidly targeted to the clustered nuclear pores, where its amino-terminal domain is required to promote the redistribution of preexisting NPCs [4].
  • Using the GFP-Nup49p system with a mutant in the NPC-associated factor Gle2p that exhibits formation of NPC clusters only at 37 degrees C, it was possible to distinguish between these two models for NPC dynamics [5].
 

Biological context of NUP49

 

Anatomical context of NUP49

  • Nic96p has been isolated previously in a complex together with the nuclear pore proteins Nsp1p, Nup49p and a p54 polypeptide [9].
  • By monitoring the distribution of the GFP-Nup49p, we could assess whether NPCs were able to move from the donor section of the nuclear envelope to that of the recipient nucleus [5].
 

Other interactions of NUP49

  • Strains mutant for Nup49p or Nup116p, or genetically depleted of Nup145p, strongly accumulated unspliced pre-tRNAs [10].
  • By fluorescence-activated cell sorting for cells with low GFP signal from a population of mutagenized cells expressing GFP-Nup49p, three complementation groups were identified: two correspond to mutant nup120 and gle2 alleles that result in clusters of NPCs [11].
  • In nup133- dividing cells that display a constitutive nuclear pore clustering, in vivo analysis of GFP-Nup49p localization revealed changes in the distribution of nuclear pore complex (NPC) clusters [4].
 

Analytical, diagnostic and therapeutic context of NUP49

References

  1. Structure and assembly of the Nup84p complex. Siniossoglou, S., Lutzmann, M., Santos-Rosa, H., Leonard, K., Mueller, S., Aebi, U., Hurt, E. J. Cell Biol. (2000) [Pubmed]
  2. A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants. Hurt, E., Hannus, S., Schmelzl, B., Lau, D., Tollervey, D., Simos, G. J. Cell Biol. (1999) [Pubmed]
  3. Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. Chial, H.J., Rout, M.P., Giddings, T.H., Winey, M. J. Cell Biol. (1998) [Pubmed]
  4. Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. Belgareh, N., Doye, V. J. Cell Biol. (1997) [Pubmed]
  5. In vivo dynamics of nuclear pore complexes in yeast. Bucci, M., Wente, S.R. J. Cell Biol. (1997) [Pubmed]
  6. The sequence of an 11.1 kb fragment on the left arm of Saccharomyces cerevisiae chromosome VII reveals six open reading frames including NSP49, KEM1 and four putative new genes. Bertani, I., Coglievina, M., Zaccaria, P., Klima, R., Bruschi, C.V. Yeast (1995) [Pubmed]
  7. A new family of yeast nuclear pore complex proteins. Wente, S.R., Rout, M.P., Blobel, G. J. Cell Biol. (1992) [Pubmed]
  8. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. Wimmer, C., Doye, V., Grandi, P., Nehrbass, U., Hurt, E.C. EMBO J. (1992) [Pubmed]
  9. Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p. Grandi, P., Schlaich, N., Tekotte, H., Hurt, E.C. EMBO J. (1995) [Pubmed]
  10. Yeast nucleoporin mutants are defective in pre-tRNA splicing. Sharma, K., Fabre, E., Tekotte, H., Hurt, E.C., Tollervey, D. Mol. Cell. Biol. (1996) [Pubmed]
  11. A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Bucci, M., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
 
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