Plant Physiology Preview
Published on September 1, 2006; 10.1104/pp.106.086975
Received July 19, 2006
Accepted August 29, 2006
Molecular identification of an Arabidopsis thaliana S-adenosylmethionine transporter: analysis of organ distribution, bacterial expression, reconstitution into liposomes and functional characterization
Luigi Palmieri , Roberto Arrigoni , Emanuela Blanco , Fernando Carrari , Maria Ines Zanor , Claudia Studart-Guimareas , Alisdair R. Fernie , and Ferdinando Palmieri *
Department of Pharmaco-Biology, Laboratory of Biochemistry and Molecular Biology, University of Bari, Via E. Orabona 4, 70125 Bari, Italy; CNR Institute of Biomembranes and Bioenergetics, Via Orabona 4, 70125 Bari, Italy
Department of Pharmaco-Biology, Laboratory of Biochemistry and Molecular Biology, University of Bari, Via E. Orabona 4, 70125 Bari, Italy
Department Willmitzer, Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, Potsdam-Golm 14476, Germany
* Corresponding author; email: fpalm{at}farmbiol.uniba.it.
Despite much study of the role of S-adenosylmethionine in the methylation of DNA, RNA and proteins and as a co-factor for a wide range of biosynthetic processes, little is known concerning the intracellular transport of this essential metabolite. Screening of the Arabidopsis thaliana genome yielded two potential homologs of yeast and human S-adenosylmethionine transporters, designated as SAMC1 and SAMC2, both of which belong to the mitochondrial carrier protein family. The SAMC1 gene is broadly expressed at the organ level, although only in specialised tissues of roots with high rates of cell division, and appears to be upregulated in response to wounding stress, whereas the SAMC2 gene is very poorly expressed in all organs/tissues analyzed. Direct transport assays with the recombinant and reconstituted SAMC1 were utilized to demonstrate that this protein displays a very narrow substrate specificity confined to S-adenosylmethionine and its closest analogs. Further experiments revealed that SAMC1 was able to function in uniport and exchange reactions and characterised the transporter as highly active but sensitive to physiologically relevant concentrations of S-adenosylhomocysteine, S-adenosylcysteine and adenosylornithine. Green fluorescent protein-based cell biological analysis demonstrated targeting of SAMC1 to mitochondria. Previous proteomic analyses identified this protein also in the chloroplast inner envelope. In keeping with these results, bioinformatics predicted a dual localization for SAMC1. These findings suggest that the provision of cytosolically synthesized S-adenosylmethionine to mitochondria and possibly also to plastids is mediated by SAMC1 according to the relative demands for this metabolite in the organelles.
This article has been cited by other articles:
|
|
|
|
 
F. Palmieri, B. Rieder, A. Ventrella, E. Blanco, P. T. Do, A. Nunes-Nesi, A. U. Trauth, G. Fiermonte, J. Tjaden, G. Agrimi, et al.
Molecular Identification and Functional Characterization of Arabidopsis thaliana Mitochondrial and Chloroplastic NAD+ Carrier Proteins
J. Biol. Chem.,
November 6, 2009;
284(45):
31249 - 31259.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
N. Linka, F. L. Theodoulou, R. P. Haslam, M. Linka, J. A. Napier, H. E. Neuhaus, and A. P.M. Weber
Peroxisomal ATP Import Is Essential for Seedling Development in Arabidopsis thaliana
PLANT CELL,
December 1, 2008;
20(12):
3241 - 3257.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Arai, M. Hayashi, and M. Nishimura
Proteomic Identification and Characterization of a Novel Peroxisomal Adenine Nucleotide Transporter Supplying ATP for Fatty Acid {beta}-Oxidation in Soybean and Arabidopsis
PLANT CELL,
December 1, 2008;
20(12):
3227 - 3240.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. Palmieri, A. Santoro, F. Carrari, E. Blanco, A. Nunes-Nesi, R. Arrigoni, F. Genchi, A. R. Fernie, and F. Palmieri
Identification and Characterization of ADNT1, a Novel Mitochondrial Adenine Nucleotide Transporter from Arabidopsis
Plant Physiology,
December 1, 2008;
148(4):
1797 - 1808.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. Ibar and A. Orellana
The Import of S-Adenosylmethionine into the Golgi Apparatus Is Required for the Methylation of Homogalacturonan
Plant Physiology,
October 1, 2007;
145(2):
504 - 512.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Thuswaldner, J. O. Lagerstedt, M. Rojas-Stutz, K. Bouhidel, C. Der, N. Leborgne-Castel, A. Mishra, F. Marty, B. Schoefs, I. Adamska, et al.
Identification, Expression, and Functional Analyses of a Thylakoid ATP/ADP Carrier from Arabidopsis
J. Biol. Chem.,
March 23, 2007;
282(12):
8848 - 8859.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
