Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7

Ziemienowicz A, Haasen D, Staiger D, Merkle T (2003)
Plant Molecular Biology 53(1/2): 201-212.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Ziemienowicz, Alicja; Haasen, Dorothea; Staiger, DorotheeUniBi; Merkle, ThomasUniBi
Abstract / Bemerkung
We characterized the Arabidopsis orthologue of the human nuclear import receptor transportin1 (TRN1). Like the human receptor, Arabidopsis TRN1 recognizes nuclear import signals on proteins that are different from the classical basic nuclear localization signals. The M9 domain of human heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is the prototype of such signals. We show that At TRN1 binds to similar domains in hnRNP-like proteins from plants. At TRN1 also interacts with human hnRNP A1 and with yeast Nab2p, two classical import cargo proteins of transportin in these organisms. Like all nuclear transport receptors of the importin-ß family, At TRN1 binds to the regulatory GTPase Ran from Arabidopsis . We demonstrated that the amino terminus of At TRN1 is necessary for this interaction. Recombinant At TRN1 conferred nuclear import of fluorescently labelled BSA-M9 peptide conjugates in permeabilized HeLa cells, functionally replacing human TRN1 in these in vitro nuclear import assays. We identified three plant substrate proteins that interact with At TRN1 and contain M9-like domains: a novel Arabidopsis hnRNP that shows high similarity to human hnRNP A1 and two small RNA-binding proteins from Arabidopsis , At GRP7 and At GRP8. Nuclear import activity of the M9-like domains of these plant proteins was demonstrated in vivo by their ability to confer partial nuclear re-localisation of a GFP fusion protein containing a nuclear export signal. In addition, fluorescently labelled At GRP7 was specifically imported into nuclei of permeabilized HeLa cells by Arabidopsis At TRN1 and human TRN1. These results suggest that the transportin-mediated nuclear import pathway is highly conserved between man, yeast and plants.
Plant Molecular Biology
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Ziemienowicz A, Haasen D, Staiger D, Merkle T. Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7. Plant Molecular Biology. 2003;53(1/2):201-212.
Ziemienowicz, A., Haasen, D., Staiger, D., & Merkle, T. (2003). Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7. Plant Molecular Biology, 53(1/2), 201-212.
Ziemienowicz, A., Haasen, D., Staiger, D., and Merkle, T. (2003). Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7. Plant Molecular Biology 53, 201-212.
Ziemienowicz, A., et al., 2003. Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7. Plant Molecular Biology, 53(1/2), p 201-212.
A. Ziemienowicz, et al., “Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7”, Plant Molecular Biology, vol. 53, 2003, pp. 201-212.
Ziemienowicz, A., Haasen, D., Staiger, D., Merkle, T.: Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7. Plant Molecular Biology. 53, 201-212 (2003).
Ziemienowicz, Alicja, Haasen, Dorothea, Staiger, Dorothee, and Merkle, Thomas. “Arabidopsis transportin1 is the nuclear import receptor for the circadian clock-regulated RNA-binding protein AtGRP7”. Plant Molecular Biology 53.1/2 (2003): 201-212.

34 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Beyond Transcription: Fine-Tuning of Circadian Timekeeping by Post-Transcriptional Regulation.
Mateos JL, de Leone MJ, Torchio J, Reichel M, Staiger D., Genes (Basel) 9(12), 2018
PMID: 30544736
Nictaba Homologs from Arabidopsis thaliana Are Involved in Plant Stress Responses.
Eggermont L, Stefanowicz K, Van Damme EJM., Front Plant Sci 8(), 2017
PMID: 29375596
Identification of potential cargo proteins of transportin protein AtTRN1 in Arabidopsis thaliana.
Yan B, Wang X, Wang Z, Chen N, Mu C, Mao K, Han L, Zhang W, Liu H., Plant Cell Rep 35(3), 2016
PMID: 26650834
Long noncoding RNA transcriptome of plants.
Liu J, Wang H, Chua NH., Plant Biotechnol J 13(3), 2015
PMID: 25615265
Age-related expression analysis of mouse liver nuclear protein binding to 3'-untranslated region of Period2 gene.
Hamada T, Miyakawa K, Kushige H, Shibata S, Kurachi S., J Physiol Sci 65(4), 2015
PMID: 25846207
Circadian rhythms and post-transcriptional regulation in higher plants.
Romanowski A, Yanovsky MJ., Front Plant Sci 6(), 2015
PMID: 26124767
Salicylic acid-dependent and -independent impact of an RNA-binding protein on plant immunity.
Hackmann C, Korneli C, Kutyniok M, Köster T, Wiedenlübbert M, Müller C, Staiger D., Plant Cell Environ 37(3), 2014
PMID: 23961939
A glycine-rich RNA-binding protein affects gibberellin biosynthesis in Arabidopsis.
Löhr B, Streitner C, Steffen A, Lange T, Staiger D., Mol Biol Rep 41(1), 2014
PMID: 24281950
Circadian oscillation and development-dependent expression of glycine-rich RNA binding proteins in tomato fruits
Müller GL, Triassi A, Alvarez CE, Falcone Ferreyra ML, Andreo CS, Lara MV, Drincovich MF., Funct Plant Biol 41(4), 2014
PMID: IND500739485
Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function.
Khan F, Daniëls MA, Folkers GE, Boelens R, Saqlan Naqvi SM, van Ingen H., Nucleic Acids Res 42(13), 2014
PMID: 24957607
Analyses of flooding tolerance of soybean varieties at emergence and varietal differences in their proteomes.
Nanjo Y, Jang HY, Kim HS, Hiraga S, Woo SH, Komatsu S., Phytochemistry 106(), 2014
PMID: 25053003
HnRNP-like proteins as post-transcriptional regulators.
Yeap WC, Namasivayam P, Ho CL., Plant Sci 227(), 2014
PMID: 25219311
Mutational definition of binding requirements of an hnRNP-like protein in Arabidopsis using fluorescence correlation spectroscopy.
Leder V, Lummer M, Tegeler K, Humpert F, Lewinski M, Schüttpelz M, Staiger D., Biochem Biophys Res Commun 453(1), 2014
PMID: 25251471
Elements of transcriptional machinery are compatible among plants and mammals.
Wolf A, Akrap N, Marg B, Galliardt H, Heiligentag M, Humpert F, Sauer M, Kaltschmidt B, Kaltschmidt C, Seidel T., PLoS One 8(1), 2013
PMID: 23326494
Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7.
Nicaise V, Joe A, Jeong BR, Korneli C, Boutrot F, Westedt I, Staiger D, Alfano JR, Zipfel C., EMBO J 32(5), 2013
PMID: 23395902
A new set of reversibly photoswitchable fluorescent proteins for use in transgenic plants.
Lummer M, Humpert F, Wiedenlübbert M, Sauer M, Schüttpelz M, Staiger D., Mol Plant 6(5), 2013
PMID: 23434876
Using the Yeast Three-Hybrid System to Identify Proteins that Interact with a Phloem-Mobile mRNA.
Cho SK, Kang IH, Carr T, Hannapel DJ., Front Plant Sci 3(), 2012
PMID: 22969782
Nucleo-cytoplasmic transport of proteins and RNA in plants.
Merkle T., Plant Cell Rep 30(2), 2011
PMID: 20960203
Reversible photoswitchable DRONPA-s monitors nucleocytoplasmic transport of an RNA-binding protein in transgenic plants.
Lummer M, Humpert F, Steuwe C, Caesar K, Schüttpelz M, Sauer M, Staiger D., Traffic 12(6), 2011
PMID: 21453442
A proteomic analysis of oligo(dT)-bound mRNP containing oxidative stress-induced Arabidopsis thaliana RNA-binding proteins ATGRP7 and ATGRP8.
Schmidt F, Marnef A, Cheung MK, Wilson I, Hancock J, Staiger D, Ladomery M., Mol Biol Rep 37(2), 2010
PMID: 19672695
The Arabidopsis nuclear pore and nuclear envelope.
Meier I, Brkljacic J., Arabidopsis Book 8(), 2010
PMID: 22303264
Getting the message across: cytoplasmic ribonucleoprotein complexes.
Bailey-Serres J, Sorenson R, Juntawong P., Trends Plant Sci 14(8), 2009
PMID: 19616989
Glycine-rich RNA-binding protein 7 affects abiotic stress responses by regulating stomata opening and closing in Arabidopsis thaliana.
Kim JS, Jung HJ, Lee HJ, Kim KA, Goh CH, Woo Y, Oh SH, Han YS, Kang H., Plant J 55(3), 2008
PMID: 18410480
Chemokine receptor CCR2 undergoes transportin1-dependent nuclear translocation.
Favre N, Camps M, Arod C, Chabert C, Rommel C, Pasquali C., Proteomics 8(21), 2008
PMID: 18846510
SAD2, an importin -like protein, is required for UV-B response in Arabidopsis by mediating MYB4 nuclear trafficking.
Zhao J, Zhang W, Zhao Y, Gong X, Guo L, Zhu G, Wang X, Gong Z, Schumaker KS, Guo Y., Plant Cell 19(11), 2007
PMID: 17993626

41 References

Daten bereitgestellt von Europe PubMed Central.

A nuclear localization domain in the hnRNP A1 protein.
Siomi H, Dreyfuss G., J. Cell Biol. 129(3), 1995
PMID: 7730395
Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins.
Siomi MC, Eder PS, Kataoka N, Wan L, Liu Q, Dreyfuss G., J. Cell Biol. 138(6), 1997
PMID: 9298975
A plant in vitro system for the nuclear import of proteins.
Merkle T, Leclerc D, Marshallsay C, Nagy F., Plant J. 10(6), 1996
PMID: 9011099
hnRNP complexes: composition, structure, and function.
Krecic AM, Swanson MS., Curr. Opin. Cell Biol. 11(3), 1999
PMID: 10395553
Karyopherin beta2 mediates nuclear import of a mRNA binding protein.
Bonifaci N, Moroianu J, Radu A, Blobel G., Proc. Natl. Acad. Sci. U.S.A. 94(10), 1997
PMID: 9144189
Nuclear export of proteins and RNAs.
Nakielny S, Dreyfuss G., Curr. Opin. Cell Biol. 9(3), 1997
PMID: 9159083
Transport between the cell nucleus and the cytoplasm.
Gorlich D, Kutay U., Annu. Rev. Cell Dev. Biol. 15(), 1999
PMID: 10611974
Functional conservation of the transportin nuclear import pathway in divergent organisms.
Siomi MC, Fromont M, Rain JC, Wan L, Wang F, Legrain P, Dreyfuss G., Mol. Cell. Biol. 18(7), 1998
PMID: 9632798
Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta.
Fridell RA, Truant R, Thorne L, Benson RE, Cullen BR., J. Cell. Sci. 110 ( Pt 11)(), 1997
PMID: 9202393
Karyopherin beta 2B participates in mRNA export from the nucleus.
Shamsher MK, Ploski J, Radu A., Proc. Natl. Acad. Sci. U.S.A. 99(22), 2002
PMID: 12384575
AtGRP7, a nuclear RNA-binding protein as a component of a circadian-regulated negative feedback loop in Arabidopsis thaliana.
Heintzen C, Nater M, Apel K, Staiger D., Proc. Natl. Acad. Sci. U.S.A. 94(16), 1997
PMID: 9238008
Pre-mRNA splicing in higher plants.
Lorkovic ZJ, Wieczorek Kirk DA, Lambermon MH, Filipowicz W., Trends Plant Sci. 5(4), 2000
PMID: 10740297
Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins.
Aitchison JD, Blobel G, Rout MP., Science 274(5287), 1996
PMID: 8849456
HASTY, the Arabidopsis ortholog of exportin 5/MSN5, regulates phase change and morphogenesis.
Bollman KM, Aukerman MJ, Park MY, Hunter C, Berardini TZ, Poethig RS., Development 130(8), 2003
PMID: 12620976
Nucleo-cytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP A1.
Weighardt F, Biamonti G, Riva S., J. Cell. Sci. 108 ( Pt 2)(), 1995
PMID: 7769000
Nuclear import in permeabilized protoplasts from higher plants has unique features.
Hicks GR, Smith HM, Lobreaux S, Raikhel NV., Plant Cell 8(8), 1996
PMID: 8776900
Identification of different roles for RanGDP and RanGTP in nuclear protein import.
Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR., EMBO J. 15(20), 1996
PMID: 8896452
Definition of a consensus transportin-specific nucleocytoplasmic transport signal.
Bogerd HP, Benson RE, Truant R, Herold A, Phingbodhipakkiya M, Cullen BR., J. Biol. Chem. 274(14), 1999
PMID: 10092666
Analysis of the genome sequence of the flowering plant Arabidopsis thaliana.
Arabidopsis Genome Initiative., Nature 408(6814), 2000
PMID: 11130711
Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm.
Pinol-Roma S, Dreyfuss G., Nature 355(6362), 1992
PMID: 1371331
The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus.
Izaurralde E, Kutay U, von Kobbe C, Mattaj IW, Gorlich D., EMBO J. 16(21), 1997
PMID: 9351834
A novel receptor-mediated nuclear protein import pathway.
Pollard VW, Michael WM, Nakielny S, Siomi MC, Wang F, Dreyfuss G., Cell 86(6), 1996
PMID: 8808633
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates.
Bachi A, Braun IC, Rodrigues JP, Pante N, Ribbeck K, von Kobbe C, Kutay U, Wilm M, Gorlich D, Carmo-Fonseca M, Izaurralde E., RNA 6(1), 2000
PMID: 10668806


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