Europe PMC

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA.

Author information

Affiliations

  • 1. European Molecular Biology Laboratory, Heidelberg, Germany.
      Authors
    • Kambach C 1
    (1 author)

ORCIDs linked to this article

The Journal of Cell Biology, 01 Jul 1992, 118(1):11-21
https://doi.org/10.1083/jcb.118.1.11 PMID: 1618898 PMCID: PMC2289521

This article is in the Europe PMC Open access subset. Refer to the copyright information in the article for licensing details.
Free full text in Europe PMC

Abstract 

Nuclear transport of the U1 snRNP-specific protein U1A has been examined. U1A moves to the nucleus by an active process which is independent of interaction with U1 snRNA. Nuclear localization requires an unusually large sequence element situated between amino acids 94 and 204 of the protein. U1A transport is not unidirectional. The protein shuttles between nucleus and cytoplasm. At equilibrium, the concentration of the protein in the nucleus and cytoplasm is not, however, determined solely by transport rates, but can be perturbed by introducing RNA sequences that can specifically bind U1A in either the nuclear or cytoplasmic compartment. Thus, U1A represents a novel class of protein which shuttles between cytoplasm and nucleus and whose intracellular distribution can be altered by the number of free binding sites for the protein present in the cytoplasm or the nucleus.

Free full text 

Logo of jcellbiolLink to Publisher's site
J Cell Biol. 1992 Jul 1; 118(1): 11–21.
PMCID: PMC2289521
PMID: 1618898

Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA

Copyright and License information Disclaimer

Abstract

Nuclear transport of the U1 snRNP-specific protein U1A has been examined. U1A moves to the nucleus by an active process which is independent of interaction with U1 snRNA. Nuclear localization requires an unusually large sequence element situated between amino acids 94 and 204 of the protein. U1A transport is not unidirectional. The protein shuttles between nucleus and cytoplasm. At equilibrium, the concentration of the protein in the nucleus and cytoplasm is not, however, determined solely by transport rates, but can be perturbed by introducing RNA sequences that can specifically bind U1A in either the nuclear or cytoplasmic compartment. Thus, U1A represents a novel class of protein which shuttles between cytoplasm and nucleus and whose intracellular distribution can be altered by the number of free binding sites for the protein present in the cytoplasm or the nucleus.

Full Text

The Full Text of this article is available as a PDF (1.8M).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Boelens W, Scherly D, Jansen EJ, Kolen K, Mattaj IW, van Venrooij WJ. Analysis of in vitro binding of U1-A protein mutants to U1 snRNA. Nucleic Acids Res. 1991 Sep 11;19(17):4611–4618. [Europe PMC free article] [Abstract] [Google Scholar]
  • Borer RA, Lehner CF, Eppenberger HM, Nigg EA. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell. 1989 Feb 10;56(3):379–390. [Abstract] [Google Scholar]
  • Breeuwer M, Goldfarb DS. Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell. 1990 Mar 23;60(6):999–1008. [Abstract] [Google Scholar]
  • Bujard H, Gentz R, Lanzer M, Stueber D, Mueller M, Ibrahimi I, Haeuptle MT, Dobberstein B. A T5 promoter-based transcription-translation system for the analysis of proteins in vitro and in vivo. Methods Enzymol. 1987;155:416–433. [Abstract] [Google Scholar]
  • Dabauvalle MC, Schulz B, Scheer U, Peters R. Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin. Exp Cell Res. 1988 Jan;174(1):291–296. [Abstract] [Google Scholar]
  • Dingwall C, Sharnick SV, Laskey RA. A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell. 1982 Sep;30(2):449–458. [Abstract] [Google Scholar]
  • Dumont JN. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J Morphol. 1972 Feb;136(2):153–179. [Abstract] [Google Scholar]
  • Eliceiri GL. Short-lived, small RNAs in the cytoplasm of HeLa cells. Cell. 1974 Sep;3(1):11–14. [Abstract] [Google Scholar]
  • Feeney RJ, Zieve GW. Nuclear exchange of the U1 and U2 snRNP-specific proteins. J Cell Biol. 1990 Apr;110(4):871–881. [Europe PMC free article] [Abstract] [Google Scholar]
  • Feeney RJ, Sauterer RA, Feeney JL, Zieve GW. Cytoplasmic assembly and nuclear accumulation of mature small nuclear ribonucleoprotein particles. J Biol Chem. 1989 Apr 5;264(10):5776–5783. [Abstract] [Google Scholar]
  • Finlay DR, Forbes DJ. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell. 1990 Jan 12;60(1):17–29. [Abstract] [Google Scholar]
  • Finlay DR, Newmeyer DD, Price TM, Forbes DJ. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol. 1987 Feb;104(2):189–200. [Europe PMC free article] [Abstract] [Google Scholar]
  • Fischer U, Lührmann R. An essential signaling role for the m3G cap in the transport of U1 snRNP to the nucleus. Science. 1990 Aug 17;249(4970):786–790. [Abstract] [Google Scholar]
  • Fischer U, Darzynkiewicz E, Tahara SM, Dathan NA, Lührmann R, Mattaj IW. Diversity in the signals required for nuclear accumulation of U snRNPs and variety in the pathways of nuclear transport. J Cell Biol. 1991 May;113(4):705–714. [Europe PMC free article] [Abstract] [Google Scholar]
  • Gaillard C, Strauss F. Ethanol precipitation of DNA with linear polyacrylamide as carrier. Nucleic Acids Res. 1990 Jan 25;18(2):378–378. [Europe PMC free article] [Abstract] [Google Scholar]
  • Garcia-Bustos J, Heitman J, Hall MN. Nuclear protein localization. Biochim Biophys Acta. 1991 Mar 7;1071(1):83–101. [Abstract] [Google Scholar]
  • Goldfarb DS. Nuclear transport. Curr Opin Cell Biol. 1989 Jun;1(3):441–446. [Abstract] [Google Scholar]
  • Goldfarb DS. Shuttling proteins go both ways. Curr Biol. 1991 Aug;1(4):212–214. [Abstract] [Google Scholar]
  • Gurdon JB. Injected nuclei in frog oocytes: fate, enlargement, and chromatin dispersal. J Embryol Exp Morphol. 1976 Dec;36(3):523–540. [Abstract] [Google Scholar]
  • Hall MN, Hereford L, Herskowitz I. Targeting of E. coli beta-galactosidase to the nucleus in yeast. Cell. 1984 Apr;36(4):1057–1065. [Abstract] [Google Scholar]
  • Hamm J, Mattaj IW. Monomethylated cap structures facilitate RNA export from the nucleus. Cell. 1990 Oct 5;63(1):109–118. [Abstract] [Google Scholar]
  • Hamm J, Dathan NA, Mattaj IW. Functional analysis of mutant Xenopus U2 snRNAs. Cell. 1989 Oct 6;59(1):159–169. [Abstract] [Google Scholar]
  • Hamm J, Dathan NA, Scherly D, Mattaj IW. Multiple domains of U1 snRNA, including U1 specific protein binding sites, are required for splicing. EMBO J. 1990 Apr;9(4):1237–1244. [Europe PMC free article] [Abstract] [Google Scholar]
  • Hamm J, Darzynkiewicz E, Tahara SM, Mattaj IW. The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal. Cell. 1990 Aug 10;62(3):569–577. [Abstract] [Google Scholar]
  • Heinrichs V, Bach M, Winkelmann G, Lührmann R. U1-specific protein C needed for efficient complex formation of U1 snRNP with a 5' splice site. Science. 1990 Jan 5;247(4938):69–72. [Abstract] [Google Scholar]
  • Kalderon D, Roberts BL, Richardson WD, Smith AE. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. [Abstract] [Google Scholar]
  • Kleinschmidt JA, Dingwall C, Maier G, Franke WW. Molecular characterization of a karyophilic, histone-binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis. EMBO J. 1986 Dec 20;5(13):3547–3552. [Europe PMC free article] [Abstract] [Google Scholar]
  • Krohne G, Waizenegger I, Höger TH. The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope. J Cell Biol. 1989 Nov;109(5):2003–2011. [Europe PMC free article] [Abstract] [Google Scholar]
  • Lamond AL. The trimethyl-guanosine cap is a nuclear targeting signal for snRNPs. Trends Biochem Sci. 1990 Dec;15(12):451–452. [Abstract] [Google Scholar]
  • Lanford RE, Butel JS. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell. 1984 Jul;37(3):801–813. [Abstract] [Google Scholar]
  • Lehmeier T, Foulaki K, Lührmann R. Evidence for three distinct D proteins, which react differentially with anti-Sm autoantibodies, in the cores of the major snRNPs U1, U2, U4/U6 and U5. Nucleic Acids Res. 1990 Nov 25;18(22):6475–6484. [Europe PMC free article] [Abstract] [Google Scholar]
  • Lerner EA, Lerner MR, Janeway CA, Jr, Steitz JA. Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. Proc Natl Acad Sci U S A. 1981 May;78(5):2737–2741. [Europe PMC free article] [Abstract] [Google Scholar]
  • Lührmann R, Kastner B, Bach M. Structure of spliceosomal snRNPs and their role in pre-mRNA splicing. Biochim Biophys Acta. 1990 Nov 30;1087(3):265–292. [Abstract] [Google Scholar]
  • Lutz-Freyermuth C, Query CC, Keene JD. Quantitative determination that one of two potential RNA-binding domains of the A protein component of the U1 small nuclear ribonucleoprotein complex binds with high affinity to stem-loop II of U1 RNA. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6393–6397. [Europe PMC free article] [Abstract] [Google Scholar]
  • Mandell RB, Feldherr CM. Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope. J Cell Biol. 1990 Nov;111(5 Pt 1):1775–1783. [Europe PMC free article] [Abstract] [Google Scholar]
  • Mattaj IW, De Robertis EM. Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins. Cell. 1985 Jan;40(1):111–118. [Abstract] [Google Scholar]
  • Mattaj IW, Zeller R. Xenopus laevis U2 snRNA genes: tandemly repeated transcription units sharing 5' and 3' flanking homology with other RNA polymerase II transcribed genes. EMBO J. 1983;2(11):1883–1891. [Europe PMC free article] [Abstract] [Google Scholar]
  • Michaud N, Goldfarb D. Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways. J Cell Biol. 1992 Feb;116(4):851–861. [Europe PMC free article] [Abstract] [Google Scholar]
  • Mount SM, Pettersson I, Hinterberger M, Karmas A, Steitz JA. The U1 small nuclear RNA-protein complex selectively binds a 5' splice site in vitro. Cell. 1983 Jun;33(2):509–518. [Abstract] [Google Scholar]
  • Nagai K, Oubridge C, Jessen TH, Li J, Evans PR. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature. 1990 Dec 6;348(6301):515–520. [Abstract] [Google Scholar]
  • Newmeyer DD, Finlay DR, Forbes DJ. In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins. J Cell Biol. 1986 Dec;103(6 Pt 1):2091–2102. [Europe PMC free article] [Abstract] [Google Scholar]
  • Pan ZQ, Prives C. Assembly of functional U1 and U2 human-amphibian hybrid snRNPs in Xenopus laevis oocytes. Science. 1988 Sep 9;241(4871):1328–1331. [Abstract] [Google Scholar]
  • Pan ZQ, Prives C. U2 snRNA sequences that bind U2-specific proteins are dispensable for the function of U2 snRNP in splicing. Genes Dev. 1989 Dec;3(12A):1887–1898. [Abstract] [Google Scholar]
  • Richardson WD, Mills AD, Dilworth SM, Laskey RA, Dingwall C. 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):655–664. [Abstract] [Google Scholar]
  • Rihs HP, Peters R. Nuclear transport kinetics depend on phosphorylation-site-containing sequences flanking the karyophilic signal of the Simian virus 40 T-antigen. EMBO J. 1989 May;8(5):1479–1484. [Europe PMC free article] [Abstract] [Google Scholar]
  • Robbins J, Dilworth SM, Laskey RA, Dingwall C. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 1991 Feb 8;64(3):615–623. [Abstract] [Google Scholar]
  • Scherly D, Boelens W, van Venrooij WJ, Dathan NA, Hamm J, Mattaj IW. Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA. EMBO J. 1989 Dec 20;8(13):4163–4170. [Europe PMC free article] [Abstract] [Google Scholar]
  • Silver PA. How proteins enter the nucleus. Cell. 1991 Feb 8;64(3):489–497. [Abstract] [Google Scholar]
  • Silver PA, Chiang A, Sadler I. Mutations that alter both localization and production of a yeast nuclear protein. Genes Dev. 1988 Jun;2(6):707–717. [Abstract] [Google Scholar]
  • Vankan P, McGuigan C, Mattaj IW. Domains of U4 and U6 snRNAs required for snRNP assembly and splicing complementation in Xenopus oocytes. EMBO J. 1990 Oct;9(10):3397–3404. [Europe PMC free article] [Abstract] [Google Scholar]
  • Zieve GW, Sauterer RA, Feeney RJ. Newly synthesized small nuclear RNAs appear transiently in the cytoplasm. J Mol Biol. 1988 Jan 20;199(2):259–267. [Abstract] [Google Scholar]
Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

Full text links 

Read article at publisher's site: https://doi.org/10.1083/jcb.118.1.11

Read article for free, from open access legal sources, via Unpaywall: http://jcb.rupress.org/content/118/1/11.full.pdfUnpaywall

Citations & impact 

Impact metrics

91
Citations
Jump to Citations
1
Data citation
Jump to Data

Citations of article over time

Article citations

Go to all (91) article citations

Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.