Home LiteratureArticle Details
PMID: 7644471 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The yeast nuclear import receptor is required for mitosis.

Loeb JD, Schlenstedt G, Pellman D, Kornitzer D, Silver PA, Fink GR

Abstract

The nuclear import system is highly conserved among eukaryotes. Here we report the effects of a conditional mutation in SRP1, which encodes a Saccharomyces cerevisiae homolog of the vertebrate nuclear import receptor importin. Importin was isolated as a factor required for the initial targeting step of a nuclear import substrate to the nuclear envelope in a mammalian in vitro assay. We show that yeast Srp1 is similarly required for protein import. In addition, Srp1 is also required for the execution of mitosis: we demonstrate that cells containing a conditional mutation of SRP1 arrest with a G2/M phenotype in a manner analogous to classic cdc mutants. This defect may be due to the failure of the mutant to degrade the mitotic cyclin Clb2 and other proteins required for mitosis. The requirement of a nuclear import receptor for cell cycle-regulated proteolysis implies that import of cell cycle regulators into the nucleus is critical for cell cycle progression.

MeSH Terms
Animals Base Sequence Cell Nucleus/physiology DNA Primers Genes, Fungal Genes, Lethal Genotype Karyopherins Mating Factor Mitosis Molecular Sequence Data Mutagenesis Nuclear Proteins/genetics,metabolism Peptides/metabolism Pheromones/metabolism Polymerase Chain Reaction Recombinant Fusion Proteins/biosynthesis Saccharomyces cerevisiae/genetics,growth & development,metabolism Vertebrates alpha Karyopherins
Chemicals
DNA Primers Karyopherins Nuclear Proteins Peptides Pheromones Recombinant Fusion Proteins alpha Karyopherins Mating Factor
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Loeb J D
Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142, USA.
Schlenstedt G
Pellman D
Kornitzer D
Silver P A
Fink G R
References (35)
35 references, click to expand
  1. A mutant nuclear protein with similarity to RNA binding proteins interferes with nuclear import in yeast.
    Mol Biol Cell. 1992 Aug;3(8):875-93 PMID: 1392078
  2. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope.
    Curr Biol. 1995 Apr 1;5(4):383-92 PMID: 7627554
  3. NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex.
    Mol Biol Cell. 1993 Feb;4(2):209-22 PMID: 8443417
  4. Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast.
    EMBO J. 1993 May;12(5):1969-78 PMID: 8491189
  5. Eviction and transplacement of mutant genes in yeast.
    Methods Enzymol. 1983;101:211-28 PMID: 6310325
  6. Two nuclear mutations that block mitochondrial protein import in yeast.
    Proc Natl Acad Sci U S A. 1984 Aug;81(15):4819-23 PMID: 6235522
  7. Amino acid sequences that determine the nuclear localization of yeast histone 2B.
    Mol Cell Biol. 1987 Nov;7(11):4048-57 PMID: 3123916
  8. Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation.
    Cell. 1988 Mar 11;52(5):641-53 PMID: 3345567
  9. Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores.
    Cell. 1988 Mar 11;52(5):655-64 PMID: 3125984
  10. Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein.
    J Cell Biol. 1988 Jul;107(1):17-31 PMID: 3292539
  11. Identification of specific binding proteins for a nuclear location sequence.
    Nature. 1989 Jan 19;337(6204):276-9 PMID: 2911368
  12. Yeast proteins that recognize nuclear localization sequences.
    J Cell Biol. 1989 Sep;109(3):983-9 PMID: 2670959
  13. Nuclear protein localization.
    Biochim Biophys Acta. 1991 Mar 7;1071(1):83-101 PMID: 2004116
  14. A yeast protein that binds nuclear localization signals: purification localization, and antibody inhibition of binding activity.
    J Cell Biol. 1991 Jun;113(6):1243-54 PMID: 2045410
  15. Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import.
    Cell. 1991 Sep 6;66(5):837-47 PMID: 1653647
  16. Regulation of p34CDC28 tyrosine phosphorylation is not required for entry into mitosis in S. cerevisiae.
    Nature. 1992 Jan 23;355(6358):368-71 PMID: 1731251
  17. A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import.
    J Cell Biol. 1992 May;117(3):473-82 PMID: 1572892
  18. The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors.
    Cell. 1992 Jun 12;69(6):939-50 PMID: 1606616
  19. CLB5: a novel B cyclin from budding yeast with a role in S phase.
    Genes Dev. 1992 Sep;6(9):1695-706 PMID: 1387626
  20. Full activation of p34CDC28 histone H1 kinase activity is unable to promote entry into mitosis in checkpoint-arrested cells of the yeast Saccharomyces cerevisiae.
    Mol Cell Biol. 1993 Jun;13(6):3744-55 PMID: 8388545
  21. Anaphase is initiated by proteolysis rather than by the inactivation of maturation-promoting factor.
    Cell. 1993 Jul 2;73(7):1393-402 PMID: 8391932
  22. CSE1 and CSE2, two new genes required for accurate mitotic chromosome segregation in Saccharomyces cerevisiae.
    Mol Cell Biol. 1993 Aug;13(8):4691-702 PMID: 8336709
  23. Reconstitution of nuclear protein transport with semi-intact yeast cells.
    J Cell Biol. 1993 Nov;123(4):785-98 PMID: 8227140
  24. S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase.
    Nature. 1993 Nov 25;366(6453):358-62 PMID: 8247132
  25. Mutations in PRG1, a yeast proteasome-related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene.
    Proc Natl Acad Sci U S A. 1994 Mar 15;91(6):2031-5 PMID: 8134345
  26. Closing the cell cycle circle in yeast: G2 cyclin proteolysis initiated at mitosis persists until the activation of G1 cyclins in the next cycle.
    Cell. 1994 Jul 1;77(7):1037-50 PMID: 8020094
  27. Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure.
    Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6880-4 PMID: 8041713
  28. Genetic and physical interactions between Srp1p and nuclear pore complex proteins Nup1p and Nup2p.
    J Cell Biol. 1994 Aug;126(3):619-30 PMID: 8045927
  29. Mitosis in transition.
    Cell. 1994 Nov 18;79(4):563-71 PMID: 7954823
  30. Isolation of a protein that is essential for the first step of nuclear protein import.
    Cell. 1994 Dec 2;79(5):767-78 PMID: 8001116
  31. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins.
    Nature. 1995 Jan 5;373(6509):78-81 PMID: 7800043
  32. Regulated degradation of the transcription factor Gcn4.
    EMBO J. 1994 Dec 15;13(24):6021-30 PMID: 7813440
  33. Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes.
    Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):2008-11 PMID: 7892216
  34. Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast.
    Cell. 1995 Apr 21;81(2):269-78 PMID: 7736579
  35. Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae.
    Mol Cell Biol. 1992 Dec;12(12):5640-51 PMID: 1448093
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1995-08-15
Pages
7647-51
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC41202
Subset
IM
Grants
NIGMS NIH HHS · GM-36373 · United States
NIGMS NIH HHS · GM-40266 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]