Isolation and characterization of two distinct classes of DXS genes in Hevea brasiliensis

Two cDNAs encoding two distinct classes of DXSs were cloned from leaves (HbDXS1) and latex (HbDXS2) of Hevea brasiliensis by RT-PCR based methods. HbDXS1 encodes a protein of 720 amino acids, with a high homology to the class I of plant DXS proteins, and HbDXS2 encodes a protein predicted to contain...

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Bibliographic Details
Published in:DNA sequence 2008-06, Vol.19 (3), p.291-300
Main Authors: Seetang-Nun, Yortyot, Sharkey, Thomas D., Suvachittanont, Wallie
Format: Article
Language:English
Subjects:
Amino Acid Sequence
DNA, Complementary - genetics
Gene Expression Regulation, Plant - drug effects
Genes, Plant - genetics
Hevea - enzymology
Hevea - genetics
Hevea brasiliensis
Models, Molecular
Molecular Sequence Data
Organophosphorus Compounds - pharmacology
Phylogeny
Plant Growth Regulators - pharmacology
Protein Structure, Tertiary
Sequence Alignment
Sequence Homology, Amino Acid
Transferases - chemistry
Transferases - classification
Transferases - genetics
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Summary:Two cDNAs encoding two distinct classes of DXSs were cloned from leaves (HbDXS1) and latex (HbDXS2) of Hevea brasiliensis by RT-PCR based methods. HbDXS1 encodes a protein of 720 amino acids, with a high homology to the class I of plant DXS proteins, and HbDXS2 encodes a protein predicted to contain 711 amino acids and with a high homology to the plant DXS class II proteins. Several important motifs and amino acid positions characteristic of DXS proteins are strictly conserved in both new HbDXS proteins. The two HbDXS genes were differentially expressed in various tissues of H. brasiliensis. The transcriptional levels of HbDXS2 were similar in both a high-yielding rubber clone (RRIM 600) and the wild type. Ethephon increased the latex yield and caused a transient increase of expression of the HbDXS2 gene. The expression of HbDXS2 in latex indicates that it may have a primary function in carotenoid biosynthesis rather than for natural rubber.
ISSN:1042-5179
1029-2365
DOI:10.1080/10425170701576768