Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula

Yaneva IA, Niehaus K (2005)
Plant Physiology and Biochemistry 43(3): 203-212.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
We have isolated and sequenced the full-length cDNA of a GDP-dissociation inhibitor (GDI) from the model legume Medicago truncatula L. The cDNA (MtGDI) contains an open reading frame of 1335 bp, coding for a protein of 444 amino acids with a calculated molecular mass of 49,785 kDa. The deduced amino acid sequence shows significant homology to other plant GDIs, the highest homology being found to GDI from the legume Cicer arietinum (96% identity). The MtGDI was expressed as a N-terminal FLAG-fusion protein in Escherichia coli BL21 (DE3). Its direct interaction with a small G protein of Rab type from Medicago sativa, MsRab11f, was demonstrated in vitro by co-immunoprecipitation using a peptide-specific antibody raised against MtGDI. The dissociation constant of the MtGDI-MsRab11f complex (4 μ M) was determined by a surface plasmon resonance (SPR) assay. Real-time RT-PCR and Western blot analyses suggested that MtGDI is ubiquitously expressed in M. truncatula. High levels of MtGDI mRNA were detected in uninfected roots, leaves and root nodules. In etiolated seedlings and cell cultures, the amount of MtGDI mRNA was much lower. In all tissues tested, the peptide-specific anti-MtGDI antibody detected the expected 50 kDa protein in the total protein extracts. MtGDI was found in the cytosol; however, a significant fraction was associated with the intracellular membranes in seedlings and roots indicating a membrane localisation of the protein. A second immunoreactive band was detected in leaves suggesting that more than one GDI isoform exist in M. truncatula. © 2005 Elsevier SAS. All rights reserved.
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Plant Physiology and Biochemistry
Band
43
Zeitschriftennummer
3
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203-212
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Yaneva IA, Niehaus K. Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula. Plant Physiology and Biochemistry. 2005;43(3):203-212.
Yaneva, I. A., & Niehaus, K. (2005). Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula. Plant Physiology and Biochemistry, 43(3), 203-212. doi:10.1016/j.plaphy.2005.01.019
Yaneva, I. A., and Niehaus, K. (2005). Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula. Plant Physiology and Biochemistry 43, 203-212.
Yaneva, I.A., & Niehaus, K., 2005. Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula. Plant Physiology and Biochemistry, 43(3), p 203-212.
I.A. Yaneva and K. Niehaus, “Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula”, Plant Physiology and Biochemistry, vol. 43, 2005, pp. 203-212.
Yaneva, I.A., Niehaus, K.: Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula. Plant Physiology and Biochemistry. 43, 203-212 (2005).
Yaneva, I. A., and Niehaus, Karsten. “Molecular cloning and characterisation of a Rab-binding GDP-dissociation inhibitor from Medicago truncatula”. Plant Physiology and Biochemistry 43.3 (2005): 203-212.

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Proteomic analysis of conidia germination in Colletotrichum acutatum.
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27 References

Daten bereitgestellt von Europe PubMed Central.

Rab-GDP dissociation inhibitor isoforms in Arabidopsis thaliana
Andreeva, J. Exp. Bot. 48(), 1997
Geno3D: automatic comparative molecular modelling of protein.
Combet C, Jambon M, Deleage G, Geourjon C., Bioinformatics 18(1), 2002
PMID: 11836238

AUTHOR UNKNOWN, 0
Nucleotide sequence of a cDNA for GDP dissociation inhibitor (GDI) which is induced by aluminum (Al) ion stress in tobacco cell culture (accession No. AF012823)
Ezaki, Plant Physiol. 115(), 1997
GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway.
Garrett MD, Zahner JE, Cheney CM, Novick PJ., EMBO J. 13(7), 1994
PMID: 8157010
Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor.
Kim WY, Kim CY, Cheong NE, Choi YO, Lee KO, Lee SH, Park JB, Nakano A, Bahk JD, Cho MJ, Lee SY., Planta 210(1), 1999
PMID: 10592042
A new functional domain of guanine nucleotide dissociation inhibitor (alpha-GDI) involved in Rab recycling.
Luan P, Heine A, Zeng K, Moyer B, Greasely SE, Kuhn P, Balch WE, Wilson IA., Traffic 1(3), 2000
PMID: 11208110
Rab proteins
Martinez, BBA 1404(), 1998
Expression of a novel chickpea Rab-GDI cDNA mainly in seedlings
Miñoz, Plant Physiol. Biochem. 39(), 2001
A revised medium for rapid growth and bioassays with tobacco tissue cultures
Murashige, Physiol. Plant. 15(), 1962
Molecular cloning and characterization of two rab GDI species from rat brain: brain-specific and ubiquitous types.
Nishimura N, Nakamura H, Takai Y, Sano K., J. Biol. Chem. 269(19), 1994
PMID: 8188702
Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase.
Rak A, Pylypenko O, Durek T, Watzke A, Kushnir S, Brunsveld L, Waldmann H, Goody RS, Alexandrov K., Science 302(5645), 2003
PMID: 14576435
Structure and mutational analysis of Rab GDP-dissociation inhibitor.
Schalk I, Zeng K, Wu SK, Stura EA, Matteson J, Huang M, Tandon A, Wilson IA, Balch WE., Nature 381(6577), 1996
PMID: 8609986
A rab-related small GTP binding protein is predominantly expressed in root nodules of Medicago sativa
Schiene, Mol. Gen. Genet. 272(), 2004
The plant Golgi apparatus: structure, functional organisation and trafficking mechanisms
Staehelin, Annu. Rev. Plant Physiol. Plant Mol. Biol. 46(), 1995
Traffic control: Rab GTPases and the regulation of interorganellar transport.
Tuvim MJ, Adachi R, Hoffenberg S, Dickey BF., News Physiol. Sci. 16(), 2001
PMID: 11390949
AtGDI2, a novel Arabidopsis gene encoding a Rab GDP dissociation inhibitor.
Ueda T, Yoshizumi T, Anai T, Matsui M, Uchimiya H, Nakano A., Gene 206(1), 1998
PMID: 9461425
Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins.
Ullrich O, Stenmark H, Alexandrov K, Huber LA, Kaibuchi K, Sasaki T, Takai Y, Zerial M., J. Biol. Chem. 268(24), 1993
PMID: 8349690
Analysis of the small GTPase gene superfamily of Arabidopsis.
Vernoud V, Horton AC, Yang Z, Nielsen E., Plant Physiol. 131(3), 2003
PMID: 12644670
MRS6--yeast homologue of the choroideraemia gene.
Waldherr M, Ragnini A, Schweyer RJ, Boguski MS., Nat. Genet. 3(3), 1993
PMID: 8387377
Structural insights into the function of the Rab GDI superfamily.
Wu SK, Zeng K, Wilson IA, Balch WE., Trends Biochem. Sci. 21(12), 1996
PMID: 9009830
Molecular role for the Rab binding platform of guanine nucleotide dissociation inhibitor in endoplasmic reticulum to Golgi transport.
Wu SK, Luan P, Matteson J, Zeng K, Nishimura N, Balch WE., J. Biol. Chem. 273(41), 1998
PMID: 9756941

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