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.

Journal Article | Published | English

No fulltext has been uploaded

Author
;
Abstract
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.
Publishing Year
ISSN
PUB-ID

Cite this

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.
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.
This data publication is cited in the following publications:
This publication cites the following data publications:

3 Citations in Europe PMC

Data provided by Europe PubMed Central.

Bacterial-induced expression of RAB18 protein in Orzya sativa salinity stress and insights into molecular interaction with GTP ligand.
Jha Y, Sablok G, Subbarao N, Sudhakar R, Fazil MH, Subramanian RB, Squartini A, Kumar S., J. Mol. Recognit. 27(9), 2014
PMID: 25042706
Proteomic analysis of conidia germination in Colletotrichum acutatum.
El-Akhal MR, Colby T, Cantoral JM, Harzen A, Schmidt J, Fernandez-Acero FJ., Arch. Microbiol. 195(4), 2013
PMID: 23371377
Survey of the year 2005 commercial optical biosensor literature.
Rich RL, Myszka DG., J. Mol. Recognit. 19(6), 2006
PMID: 17125150

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 15854828
PubMed | Europe PMC

Search this title in

Google Scholar