S-adenosyl-L-homocystein hydrolase promoter

Details S-adenosyl-L-homocystein hydrolase promoter S-adenosyl-L-homocystein hydrolase promoter

1997-10-09

2000-03-14

Fox, David T.

Multicellular living organisms and unmodified parts thereof and

Method of introducing a polynucleotide molecule into or...

The polynucleotide contains a tissue, organ, or cell...

800279, 800288, 800294, 800298, 800306, 8003172, 8003173, 8003174, 8003201, 8003203, 435411, 435412, 435414, 435417, 435418, 435419, 435421, 435468, 435469, 4353201, 536 236, 536 241, C12N 1529, C12N 1582, C12N 1584, A01H 500

Patent

active

060375248

DESCRIPTION:

BRIEF SUMMARY
FIELD OF THE INVENTION

The present invention relates to a promoter sequence capable of giving a high level of expression within plant cells. In particular, it relates to a promoter derived from a gene encoding S-adenosyl-L-homocysteine hydrolase (SHH).


BACKGROUND OF THE INVENTION

Promoters control the spatial and temporal expression of genes by modulating their level of transcription. Early approaches to genetically engineered crop plants utilised strong constitutive promoters to drive the expression of foreign genes. As strategies in plant biotechnology have become more sophisticated, specific promoters have been used to target transgene expression to a particular tissue or to a particular developmental stage. The promoter of the present invention is especially versatile as it can be used either to give constitutive expression of a gene or to target increased levels of gene expression at sites of wounding or pathogen invasion.
SHH was first described, in rat liver extracts, as the activity responsible for the reversible hydrolysis of S-adenosyl-L-homocysteine (SAH) to adenosine and homocysteine by the cleavage of a thioether bond in SAH [de la Haba, G. and Cantoni, G. L. (1959). J. Biol. Chem. 234, 603-608].
SAH is formed as a direct product of transmethylation reactions involving S-adenosyl-L-methionine (SAM) [Cantoni, G. L. and Scarano, E. (1954). J. Am. Chem. Soc. 76, 4744] and is known to be a potent inhibitor of most SAM mediated methyltransfer reactions. Therefore SAH is converted to homocysteine and adenosine by SHH as shown schematically below:


______________________________________ S-adenosyl-L-methionine (SAM) .uparw..dwnarw. Methyltransferase Methylated Product + S-adenosyl-L-homocysteine (SAH) .uparw..dwnarw. SHH Adenosine + L-homocysteine .uparw..dwnarw. N5-methyltetrahydrofolate Methionine ______________________________________ SHH has been found in all cells tested with the exception of Escherichia coli and other related bacteria [Shimzu, S. et al. (1984). Eur. J. Biochem. 141, 385-392].
The unique metabolic role of SHH in the removal of SAH and the structural complexity of the enzyme suggest that SHH may have a role in the regulation of the biological utilisation of SAM. SAM serves as a major methyl group donor for numerous highly specific methyltransferase reactions with a large variety of acceptor molecules; for example phenylpropanoid derivatives, cyclic fatty acids, proteins, polysaccharides and nucleic acids [Tabor, C. W. and Tabor, H. (1984). Adv. Enzymol. 56, 251-282]. It should be noted that SAM also has regulatory functions, namely the allosteric stimulation of threonine synthase. In plants, SHH has been studied primarily in relation to the biosynthesis of various phenylpropanoid derivatives.
Enzymes affecting the intracellular levels of SAH are important in the study of plant methylation reactions because it has been demonstrated that many methyltransferases are inhibited by SAH [Deguchi, T. and Barchos, J. (1971). J. Biol. Chem. 246, 3175-3181]. For example, an enzyme catalysing the methylation of caffeic acid was purified from spinach-beet leaves and found to be potently inhibited by SAH [Poulton, J. E. and Butt, V. S. (1976). Arch. of Biochem. Biophys. 172, 135-142]. Other metabolic pathways of the plant which involve transmethylation are the production of lignin and suberin, which are both derived from phenylalanine, through a series of reactions. These reactions include the methylation of caffeic acid into ferulic acid and also the methylation of s-hydroxyferulic acid into sinapic acid. Both these methylation reactions require SAM and hence produce SAH as a byproduct which needs to be removed by SHH to allow further transmethylation.
Once SHH had been isolated, many factors were calculated, such as the enzyme's pH optimum of 8.5, with a 50% activity between pH 6.5-10. Due to the Km value found for the substrate, L-homocysteine, the synthesis of SAH proceeds in vivo at a significant rate only when L-homocysteine is accumulated [Poulton, J. E.

REFERENCES:
Merta et al. The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase. European Journal of Biochemistry. 229:575-582, Apr. 1995.
Schroder et al. cDNA for S-adenosyl-L-homocysteine hydrolase from Catharanthus roseus. Plant Physiology. 104:1099-1100, 1994.
Database WPI; Section Ch, Week 9243; Derwent Publications ltd., London, GB; Class C06, AN 92-354683 XP00201269 & JP, A, 04 258 292 (Japan Tobacco Inc), Sep. 14, 1992.
Cantoni et al; The Formation of S-Adenosylho-Mocysteine in Enzymatic Transmethylation Reactions; vol. 76, p. 4744.
Jefferson et al; GUS fusions .beta.-glucuronidase as a sensitive and versatile gene fusion maker in higher plants The EMBO Journal vol. 6, pp. 3901-3907 (1987).
OW et al; Transient and Stable Expression of the Firefly Luciferase Gene in Plant Cells and Transgenic Plants; Science Reports, Nov. 14, 1986, vol. 234; pp. 856-859.
Warner et al.; The Development Expression of the Asparagus Intracellular PR Protein (AoPR1) Gene Correlates With Sites of Phenylpro-Panoid Biosynthesis; The Plant Journal, pp. 31-43, (1994).
Paul et al.; Dedifferentiation of Asparagus Officinalis L. Mesophyll Cells During Intiation of Cell Cultures; Plant Science, 65 pp. 111-117 (1989).
Harikrishna et al.; Wound Response in Mechanically Isolated Asparagus Mesophyll Cells: A Model Monocotyledon System; Journal of Experimental Botany, vol. 42, pp. 791-799, Jun. 1991.
Sganga et al.; Mutational and Nucleotide Sequence Analysis of S-Adenosyl-L-Homocysteine Hydrolase From Rhodobacter capsulatus ; Proc. Natl. Acad. Sci. USA; vol. 89, pp. 6328-6332, Jul. 1992.
Kawalleck et al.; Induction by Fungal Elicitor of S-Adenosyl-L-Methionine Synthetase and S-Adenosyl-L-Homocysteine Hydrolase mRNAs in Cultured Cells and Leaves of Petroselinum crispum; Natl. Acad. Sci, USA; vol. 89, pp. 4713-4717, May 1992.
Kasir et al.; Amino Acid Sequence of S-Adenosyl-L-Homocysteine Hydrolase From Dictyostelium Discoideum as Deduced From the Cdna Sequence; Biochemical and Biophysical Research Communications, vol. 153, pp. 359-364, (1988).
Ogawa et al.; Amino Acid Sequence of S-Adenosyl-L-Homocysteine Hydrolase From Rat Liver as Derived From the cDNA Sequence; Proc. Nat'l. Acad. Sci, USA; vol. 84, pp. 719-723, Feb. 1987.
Deguchi et al.; Inhibition of Transmethylations of Biogenic Amines by Adenosylhomocysteinase; The Journal of Biological Chemistry; vol. 10, pp. 3175-3318, 1971.
Jakubowski et al.; S-Adenosylhomocysteinase From Yellow Lupin Seeds: Stoichiometry and Reactions of the Enzyme-Adenosine Complex; Biochemistry 1 20, pp. 6877-6881, 1981.
Trezzini et al.; Isolation of Putative Defense-Related Genes From Arabidopsis thaliana and Expression in Fungal Elicitor-Treated Cells; Plant Molecular Biology; vol. 21, pp. 385-389, 1993.
Tanaka et al.; Inducible Expression by Plant Hormones of S-Adenosyl-L-Homocysteine Hydrolase Gene From Nicotiana tabacum During Early Flower Bud Formation In Vitro; Plant Science 113, pp. 167-174, 1996.
Skipsey et al.; The Cloning and Characterisation of S-Adenosyl-L-Homocysteine Hydrolase; Journal of Experimental Botany 45, 12, 1994.
Merta et al.; The Gene and Pseudogenes of Rat S-Adenosyl-L-Homocysteine Hydrolase; European Journal of Biochemistry; 229, pp. 575-582; Apr. 1995.
Buggy et al.; Nucleotide Sequence and Characterization of the Rhodobacter capsulatus HvrB Gene: HvrB is an Activator of S-Adenosyl-L-Homocysteine Hydrolase Expression and is a Membrane of the LysR Family; Journal of Bacteriology 176, pp. 61-69, (1994).
Clarke et al.; High-Frequency Transformation of Arabidopsis thaliana by Agrobacterium Tumefaciens; Plant Molecular Biology Reporter; vol. 10, pp. 178-189 (1992).
Tabor et al.; Methionine Adenosyltransferase (S-Adenosylmethionine Synthetase) and S-Adenosylmethionine Decarboxylase; pp. 251-282.

Affiliated with

Also associated with

Rating

S-adenosyl-L-homocystein hydrolase promoter does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with S-adenosyl-L-homocystein hydrolase promoter, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and S-adenosyl-L-homocystein hydrolase promoter will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-171052