Molecular characterization of a cDNA encoding caffeoyl-coenzyme A 3-O-methyltransferase
Abstract. A cDNA clone encoding S-adenosyl-L-methionine: trans-caffeoyl-CoA 3-O-methyl-transferase (EC 2·1·1·104; CCoAOMT) from Stellana longipes Goldie (long-stalked chick-weed) was isolated and studied. Structural analysis of both the nucleotide sequence and the predicted amino acid sequence sugge...
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| Format: | Text |
| Language: | English |
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1996
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| Online Access: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.510.8626 http://www.ias.ac.in/jarch/jbiosci/22/161-175.pdf |
| Summary: | Abstract. A cDNA clone encoding S-adenosyl-L-methionine: trans-caffeoyl-CoA 3-O-methyl-transferase (EC 2·1·1·104; CCoAOMT) from Stellana longipes Goldie (long-stalked chick-weed) was isolated and studied. Structural analysis of both the nucleotide sequence and the predicted amino acid sequence suggests that our cloned sequence encoded a CCoAOMT enzyme of Stellaria longipes, which shared overall structural similarity with other plant CCoAOMTs but exhibited certain distinct characteristics. Southern blot hybridization and cloning analyses indicating a small CCoAOMT gene family in the Stellana longipes genome and the absence of introns in the coding region of the cDNA- corresponding gene. Sequence variations in the coding region were found among three genotypes from geographically isolated populations. Higher levels of CCoAOMT mRNA were detected in stems and leaves than in roots. The cDNA-encoded protein expressed in Eschendia coli was shown to utilize caffeoyl-CoA, but not caffeic acid or 5-hydroxy ferulic acid, as its substrate. |
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