HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 275, Issue 24, 18482-18488, June 16, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/24/18482    most recent M002000200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Oh, S. K. Articles by Kang, H. Search for Related Content PubMed PubMed Citation Articles by Oh, S. K. Articles by Kang, H. Social Bookmarking                      What's this?

Molecular Cloning, Expression, and Functional Analysis of a cis-Prenyltransferase from Arabidopsis thaliana
IMPLICATIONS IN RUBBER BIOSYNTHESIS^*

Soo Kyung Oh, Kyung Hwan Han, Stephen B. Ryu, and Hunseung Kang^§

From the Kumho Life and Environmental Science Laboratory, 1 Oryong-Dong, Puk-Gu, Kwangju, 500-712, Korea

cis-Prenyltransferase catalyzes the sequential condensation of isopentenyl diphosphate with allylic diphosphate to synthesize polyprenyl diphosphates that play vital roles in cellular activity. Despite potential significance of cis-prenyltransferase in plant growth and development, no gene of the enzyme has been cloned from higher plants. Using sequence information of the conserved region of cis-prenyltransferase cloned recently from Escherichia coli, Micrococcus luteus, and yeast, we have isolated and characterized the first plant cis-prenyltransferase from Arabidopsis thaliana. Sequence analysis revealed that the protein is highly homologous in several conserved regions to cis-prenyltransferases from M. luteus, E. coli, and yeast. In vitro analyses using the recombinant protein overexpressed in E. coli revealed that the enzyme catalyzed the formation of polyprenyl diphosphates ranging in carbon number from 100 to 130 with a predominance of C₁₂₀. The enzyme exhibited a higher affinity for farnesyl diphosphate than for geranylgeranyl diphosphate, with the K_m values being 0.13 and 3.62 µM, respectively, but a lower affinity for isopentenyl diphosphate, with a K_m value of 23 µM. In vitro rubber biosynthesis analysis indicated that the Arabidopsis cis-prenyltransferase itself could not catalyze the formation of higher molecular weight polyprenyl diphosphates similar to natural rubber. A reverse transcriptase-polymerase chain reaction analysis showed that the gene was expressed at low levels in Arabidopsis plant, in which expression of the cis-prenyltransferase in leaf and root was higher than that in stem, flower, and silique. These results indicate the tissue-specific expression of cis-prenyltransferase and suggest a potential role and significance of the enzyme in the polyisoprenoid biosynthesis in plants.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF162441.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. Skorupinska-Tudek, J. Poznanski, J. Wojcik, T. Bienkowski, I. Szostkiewicz, M. Zelman-Femiak, A. Bajda, T. Chojnacki, O. Olszowska, J. Grunler, et al. Contribution of the Mevalonate and Methylerythritol Phosphate Pathways to the Biosynthesis of Dolichols in Plants J. Biol. Chem., July 25, 2008; 283(30): 21024 - 21035. [Abstract] [Full Text] [PDF]

				H. Zhang, K. Ohyama, J. Boudet, Z. Chen, J. Yang, M. Zhang, T. Muranaka, C. Maurel, J.-K. Zhu, and Z. Gong Dolichol Biosynthesis and Its Effects on the Unfolded Protein Response and Abiotic Stress Resistance in Arabidopsis PLANT CELL, July 1, 2008; 20(7): 1879 - 1898. [Abstract] [Full Text] [PDF]

				M. E. Veatch-Blohm, D. T. Ray, and W. B. McCloskey Water-Stress-Induced Changes in Resin and Rubber Concentration and Distribution in Greenhouse-Grown Guayule Agron. J., May 3, 2006; 98(3): 766 - 773. [Abstract] [Full Text] [PDF]

				K. Yi, C. Guo, D. Chen, B. Zhao, B. Yang, and H. Ren Cloning and Functional Characterization of a Formin-Like Protein (AtFH8) from Arabidopsis Plant Physiology, June 1, 2005; 138(2): 1071 - 1082. [Abstract] [Full Text] [PDF]

				I. J. Kim, S. B. Ryu, Y. S. Kwak, and H. Kang A novel cDNA from Parthenium argentatum Gray enhances the rubber biosynthetic activity in vitro* J. Exp. Bot., February 1, 2004; 55(396): 377 - 385. [Abstract] [Full Text] [PDF]

				Y. Khare, Y.-W. Zhang, M. Fujihashi, K. Miki, and T. Koyama Significance of Highly Conserved Aromatic Residues in Micrococcus luteus B-P 26 Undecaprenyl Diphosphate Synthase J. Biochem., December 1, 2003; 134(6): 819 - 826. [Abstract] [Full Text] [PDF]

				S.-Y. Chang, T.-P. Ko, P.-H. Liang, and A. H.-J. Wang Catalytic Mechanism Revealed by the Crystal Structure of Undecaprenyl Pyrophosphate Synthase in Complex with Sulfate, Magnesium, and Triton J. Biol. Chem., August 1, 2003; 278(31): 29298 - 29307. [Abstract] [Full Text] [PDF]

				A. P. Singh, S. G. Wi, G. C. Chung, Y. S. Kim, and H. Kang The micromorphology and protein characterization of rubber particles in Ficus carica, Ficus benghalensis and Hevea brasiliensis J. Exp. Bot., March 1, 2003; 54(384): 985 - 992. [Abstract] [Full Text] [PDF]

				Y.-H. Chen, A. P.-C. Chen, C.-T. Chen, A. H.-J. Wang, and P.-H. Liang Probing the Conformational Change of Escherichia coli Undecaprenyl Pyrophosphate Synthase during Catalysis Using an Inhibitor and Tryptophan Mutants J. Biol. Chem., February 22, 2002; 277(9): 7369 - 7376. [Abstract] [Full Text] [PDF]

				B. Schenk, F. Fernandez, and C. J. Waechter The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum Glycobiology, May 1, 2001; 11(5): 61R - 70R. [Abstract] [Full Text] [PDF]

				B. Schenk, J. S. Rush, C. J. Waechter, and M. Aebi An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols Glycobiology, January 1, 2001; 11(1): 89 - 98. [Abstract] [Full Text] [PDF]

				Y. Kharel, Y.-W. Zhang, M. Fujihashi, K. Miki, and T. Koyama Identification of Significant Residues for Homoallylic Substrate Binding of Micrococcus luteus B-P 26 Undecaprenyl Diphosphate Synthase J. Biol. Chem., July 20, 2001; 276(30): 28459 - 28464. [Abstract] [Full Text] [PDF]