Home LiteratureArticle Details
PMID: 1618898 Published · ppublish English Journal Article

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

The Journal of cell biology ·Vol. 118 ·No. 1 ·1992-07-00 ·Pages 11-21

Kambach C, Mattaj IW

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.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Biological Transport, Active Cell Nucleus/metabolism DNA Mutational Analysis Molecular Sequence Data Oocytes RNA, Small Nuclear/metabolism RNA-Binding Proteins Ribonucleoprotein, U1 Small Nuclear Ribonucleoproteins/genetics,metabolism Structure-Activity Relationship Subcellular Fractions/chemistry Xenopus laevis
Chemicals
RNA, Small Nuclear RNA-Binding Proteins Ribonucleoprotein, U1 Small Nuclear Ribonucleoproteins U1A protein
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kambach C
European Molecular Biology Laboratory, Heidelberg, Germany.
Mattaj I W
References (51)
51 references, click to expand
  1. 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):851-61 PMID: 1531146
  2. U2 snRNA sequences that bind U2-specific proteins are dispensable for the function of U2 snRNP in splicing.
    Genes Dev. 1989 Dec;3(12A):1887-98 PMID: 2559872
  3. Nuclear protein localization.
    Biochim Biophys Acta. 1991 Mar 7;1071(1):83-101 PMID: 2004116
  4. 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):1775-83 PMID: 2229173
  5. 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):6475-84 PMID: 1701240
  6. Analysis of in vitro binding of U1-A protein mutants to U1 snRNA.
    Nucleic Acids Res. 1991 Sep 11;19(17):4611-8 PMID: 1832492
  7. 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):705-14 PMID: 1827444
  8. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence.
    Cell. 1991 Feb 8;64(3):615-23 PMID: 1991323
  9. The trimethyl-guanosine cap is a nuclear targeting signal for snRNPs.
    Trends Biochem Sci. 1990 Dec;15(12):451-2 PMID: 2150241
  10. Structure of spliceosomal snRNPs and their role in pre-mRNA splicing.
    Biochim Biophys Acta. 1990 Nov 30;1087(3):265-92 PMID: 2147394
  11. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A.
    Nature. 1990 Dec 6;348(6301):515-20 PMID: 2147232
  12. Domains of U4 and U6 snRNAs required for snRNP assembly and splicing complementation in Xenopus oocytes.
    EMBO J. 1990 Oct;9(10):3397-404 PMID: 2145149
  13. Monomethylated cap structures facilitate RNA export from the nucleus.
    Cell. 1990 Oct 5;63(1):109-18 PMID: 2208274
  14. The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope.
    J Cell Biol. 1989 Nov;109(5):2003-11 PMID: 2808518
  15. Nuclear transport.
    Curr Opin Cell Biol. 1989 Jun;1(3):441-6 PMID: 2483331
  16. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.
    J Cell Biol. 1987 Feb;104(2):189-200 PMID: 3805121
  17. 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
  18. Cytoplasmic assembly and nuclear accumulation of mature small nuclear ribonucleoprotein particles.
    J Biol Chem. 1989 Apr 5;264(10):5776-83 PMID: 2522439
  19. A T5 promoter-based transcription-translation system for the analysis of proteins in vitro and in vivo.
    Methods Enzymol. 1987;155:416-33 PMID: 2828874
  20. Assembly of functional U1 and U2 human-amphibian hybrid snRNPs in Xenopus laevis oocytes.
    Science. 1988 Sep 9;241(4871):1328-31 PMID: 2970672
  21. 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):4163-70 PMID: 2531658
  22. 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):1479-84 PMID: 2670556
  23. Functional analysis of mutant Xenopus U2 snRNAs.
    Cell. 1989 Oct 6;59(1):159-69 PMID: 2790958
  24. Major nucleolar proteins shuttle between nucleus and cytoplasm.
    Cell. 1989 Feb 10;56(3):379-90 PMID: 2914325
  25. Newly synthesized small nuclear RNAs appear transiently in the cytoplasm.
    J Mol Biol. 1988 Jan 20;199(2):259-67 PMID: 3351925
  26. 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):291-6 PMID: 3335228
  27. A short amino acid sequence able to specify nuclear location.
    Cell. 1984 Dec;39(3 Pt 2):499-509 PMID: 6096007
  28. 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):3547-52 PMID: 3549279
  29. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored.
    Cell. 1990 Jan 12;60(1):17-29 PMID: 2295087
  30. Ethanol precipitation of DNA with linear polyacrylamide as carrier.
    Nucleic Acids Res. 1990 Jan 25;18(2):378 PMID: 2326177
  31. Nuclear exchange of the U1 and U2 snRNP-specific proteins.
    J Cell Biol. 1990 Apr;110(4):871-81 PMID: 2139037
  32. 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):6393-7 PMID: 1696729
  33. Facilitated nuclear transport of histone H1 and other small nucleophilic proteins.
    Cell. 1990 Mar 23;60(6):999-1008 PMID: 1690602
  34. The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal.
    Cell. 1990 Aug 10;62(3):569-77 PMID: 2143105
  35. An essential signaling role for the m3G cap in the transport of U1 snRNP to the nucleus.
    Science. 1990 Aug 17;249(4970):786-90 PMID: 2143847
  36. Multiple domains of U1 snRNA, including U1 specific protein binding sites, are required for splicing.
    EMBO J. 1990 Apr;9(4):1237-44 PMID: 2138978
  37. 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 PMID: 2136774
  38. The U1 small nuclear RNA-protein complex selectively binds a 5' splice site in vitro.
    Cell. 1983 Jun;33(2):509-18 PMID: 6190573
  39. 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):1883-91 PMID: 6196192
  40. Targeting of E. coli beta-galactosidase to the nucleus in yeast.
    Cell. 1984 Apr;36(4):1057-65 PMID: 6323016
  41. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen.
    Cell. 1984 Jul;37(3):801-13 PMID: 6086146
  42. A polypeptide domain that specifies migration of nucleoplasmin into the nucleus.
    Cell. 1982 Sep;30(2):449-58 PMID: 6814762
  43. 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):2737-41 PMID: 6789322
  44. Injected nuclei in frog oocytes: fate, enlargement, and chromatin dispersal.
    J Embryol Exp Morphol. 1976 Dec;36(3):523-40 PMID: 1010977
  45. Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals.
    J Morphol. 1972 Feb;136(2):153-79 PMID: 4109871
  46. Short-lived, small RNAs in the cytoplasm of HeLa cells.
    Cell. 1974 Sep;3(1):11-4 PMID: 4415761
  47. Shuttling proteins go both ways.
    Curr Biol. 1991 Aug;1(4):212-4 PMID: 15336122
  48. Mutations that alter both localization and production of a yeast nuclear protein.
    Genes Dev. 1988 Jun;2(6):707-17 PMID: 3138162
  49. In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins.
    J Cell Biol. 1986 Dec;103(6 Pt 1):2091-102 PMID: 3097026
  50. Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins.
    Cell. 1985 Jan;40(1):111-8 PMID: 2578319
  51. How proteins enter the nucleus.
    Cell. 1991 Feb 8;64(3):489-97 PMID: 1991319
Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1992-07-00
Pages
11-21
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289521
Subset
IM
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: product@genelibs.com