Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p

R. Pries; K. Bömeke; O. Draht; M. Künzler; G. H. Braus

doi:10.1007/s00438-003-0955-7

Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p

R. Pries, K. Bömeke, O. Draht, M. Künzler, G. H. Braus^*

^*Corresponding author for this work

Clinic of Otorhinolaryngology

7 Citations (Scopus)

Abstract

The yeast transcription factor Gcn4p contains two stretches of amino acid residues, NLS1 and NLS2, which are independently able to relocate the cytoplasmic protein chorismate mutase into the nucleus. Only NLS2 is conserved among fungi. A truncated version of CPCA (the counterpart of Gcn4p in Aspergillus nidulans), which lacks the conserved NLS, accumulates in the cytoplasm instead of the nucleus. Nuclear uptake mediated by the NLS1 of Gcn4p is impaired by defects in genes for several different karyopherins, whereas NLS2-dependent nuclear import specifically requires the α-importin Srp1p and the β-importin Kap95p. Yeast strains that are defective in either of these two karyopherins are unable to respond to amino acid starvation. We have thus identified Gcn4p as a substrate for the Srp1p/Kap95p transport complex. Our data suggest that NLS2 is the essential and specific nuclear transport signal; NLS1 may play only an unspecific or accessory role.

Original language	English
Journal	Molecular Genetics and Genomics
Volume	271
Issue number	3
Pages (from-to)	257-266
Number of pages	10
ISSN	1617-4615
DOIs	https://doi.org/10.1007/s00438-003-0955-7
Publication status	Published - 04.2004

Funding

Acknowledgements We thank L.F. Pemberton for the kap114 strain and Claudi Wagner for critical reading of the manuscript and exhilarating discussions. This work was supported by grants from the Deutsche Forschungsgemeinschaft, the Volkswagenstiftung and the Fonds der Chemischen Industrie

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SDG 3 Good Health and Well-being

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title = "Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p",

abstract = "The yeast transcription factor Gcn4p contains two stretches of amino acid residues, NLS1 and NLS2, which are independently able to relocate the cytoplasmic protein chorismate mutase into the nucleus. Only NLS2 is conserved among fungi. A truncated version of CPCA (the counterpart of Gcn4p in Aspergillus nidulans), which lacks the conserved NLS, accumulates in the cytoplasm instead of the nucleus. Nuclear uptake mediated by the NLS1 of Gcn4p is impaired by defects in genes for several different karyopherins, whereas NLS2-dependent nuclear import specifically requires the α-importin Srp1p and the β-importin Kap95p. Yeast strains that are defective in either of these two karyopherins are unable to respond to amino acid starvation. We have thus identified Gcn4p as a substrate for the Srp1p/Kap95p transport complex. Our data suggest that NLS2 is the essential and specific nuclear transport signal; NLS1 may play only an unspecific or accessory role.",

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note = "Funding Information: Acknowledgements We thank L.F. Pemberton for the kap114 strain and Claudi Wagner for critical reading of the manuscript and exhilarating discussions. This work was supported by grants from the Deutsche Forschungsgemeinschaft, the Volkswagenstiftung and the Fonds der Chemischen Industrie",

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AU - Pries, R.

AU - Bömeke, K.

AU - Draht, O.

AU - Künzler, M.

AU - Braus, G. H.

N1 - Funding Information: Acknowledgements We thank L.F. Pemberton for the kap114 strain and Claudi Wagner for critical reading of the manuscript and exhilarating discussions. This work was supported by grants from the Deutsche Forschungsgemeinschaft, the Volkswagenstiftung and the Fonds der Chemischen Industrie

PY - 2004/4

Y1 - 2004/4

N2 - The yeast transcription factor Gcn4p contains two stretches of amino acid residues, NLS1 and NLS2, which are independently able to relocate the cytoplasmic protein chorismate mutase into the nucleus. Only NLS2 is conserved among fungi. A truncated version of CPCA (the counterpart of Gcn4p in Aspergillus nidulans), which lacks the conserved NLS, accumulates in the cytoplasm instead of the nucleus. Nuclear uptake mediated by the NLS1 of Gcn4p is impaired by defects in genes for several different karyopherins, whereas NLS2-dependent nuclear import specifically requires the α-importin Srp1p and the β-importin Kap95p. Yeast strains that are defective in either of these two karyopherins are unable to respond to amino acid starvation. We have thus identified Gcn4p as a substrate for the Srp1p/Kap95p transport complex. Our data suggest that NLS2 is the essential and specific nuclear transport signal; NLS1 may play only an unspecific or accessory role.

AB - The yeast transcription factor Gcn4p contains two stretches of amino acid residues, NLS1 and NLS2, which are independently able to relocate the cytoplasmic protein chorismate mutase into the nucleus. Only NLS2 is conserved among fungi. A truncated version of CPCA (the counterpart of Gcn4p in Aspergillus nidulans), which lacks the conserved NLS, accumulates in the cytoplasm instead of the nucleus. Nuclear uptake mediated by the NLS1 of Gcn4p is impaired by defects in genes for several different karyopherins, whereas NLS2-dependent nuclear import specifically requires the α-importin Srp1p and the β-importin Kap95p. Yeast strains that are defective in either of these two karyopherins are unable to respond to amino acid starvation. We have thus identified Gcn4p as a substrate for the Srp1p/Kap95p transport complex. Our data suggest that NLS2 is the essential and specific nuclear transport signal; NLS1 may play only an unspecific or accessory role.

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SN - 1617-4615

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Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p

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UN SDGs

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