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A bifunctional oleate 12-hydroxylase: desaturase from Lesquerella fendleri.
Plant J. 1998 Jan; 13(2):201-10.PJ

Abstract

LFAH12, an oleate 12-hydroxylase gene from Lesquerella fendleri (L.) was isolated on the basis of nucleotide sequence similarity to an oleate hydroxylase gene from Ricinus communis (L.). Transgenic Arabidopsis plants containing the Lesquerella gene under transcriptional control of the cauliflower mosaic virus 35S promoter accumulated ricinoleic, lesquerolic and densipolic acids in seeds, but not in leaves or roots. However, hydroxylase activity was detectable in crude extracts of vegetative tissues. The discrepancy between the presence of activity and the lack of hydroxy fatty acids suggests selective removal and breakdown of hydroxy fatty acids in vegetative organs. High levels of LFAH12 mRNA accumulation did not lead to correspondingly high levels of protein accumulation, suggesting that accumulation of the hydroxylase may be controlled post-transcriptionally. Expression of the L. fendleri gene in transgenic plants of a fad2 mutant of Arabidopsis, which is deficient in cytoplasmic oleate delta 12 desaturase activity, resulted in partial suppression of the mutant phenotype in roots. Thus, unlike the hydroxylase from R. communis, the L. fendleri enzyme has both hydroxylase and desaturase activities. Fusion of the 5' flanking region of the LFAH12 gene to the beta-glucuronidase coding sequence resulted in a high level of early seed-specific expression of beta-glucuronidase activity in transgenic Arabidopsis plants.

Authors+Show Affiliations

Carnegie Institution of Washington, Department of Plant Biology, Stanford, CA 94305, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

9680976

Citation

Broun, P, et al. "A Bifunctional Oleate 12-hydroxylase: Desaturase From Lesquerella Fendleri." The Plant Journal : for Cell and Molecular Biology, vol. 13, no. 2, 1998, pp. 201-10.
Broun P, Boddupalli S, Somerville C. A bifunctional oleate 12-hydroxylase: desaturase from Lesquerella fendleri. Plant J. 1998;13(2):201-10.
Broun, P., Boddupalli, S., & Somerville, C. (1998). A bifunctional oleate 12-hydroxylase: desaturase from Lesquerella fendleri. The Plant Journal : for Cell and Molecular Biology, 13(2), 201-10.
Broun P, Boddupalli S, Somerville C. A Bifunctional Oleate 12-hydroxylase: Desaturase From Lesquerella Fendleri. Plant J. 1998;13(2):201-10. PubMed PMID: 9680976.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A bifunctional oleate 12-hydroxylase: desaturase from Lesquerella fendleri. AU - Broun,P, AU - Boddupalli,S, AU - Somerville,C, PY - 1998/7/29/pubmed PY - 1998/7/29/medline PY - 1998/7/29/entrez SP - 201 EP - 10 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 13 IS - 2 N2 - LFAH12, an oleate 12-hydroxylase gene from Lesquerella fendleri (L.) was isolated on the basis of nucleotide sequence similarity to an oleate hydroxylase gene from Ricinus communis (L.). Transgenic Arabidopsis plants containing the Lesquerella gene under transcriptional control of the cauliflower mosaic virus 35S promoter accumulated ricinoleic, lesquerolic and densipolic acids in seeds, but not in leaves or roots. However, hydroxylase activity was detectable in crude extracts of vegetative tissues. The discrepancy between the presence of activity and the lack of hydroxy fatty acids suggests selective removal and breakdown of hydroxy fatty acids in vegetative organs. High levels of LFAH12 mRNA accumulation did not lead to correspondingly high levels of protein accumulation, suggesting that accumulation of the hydroxylase may be controlled post-transcriptionally. Expression of the L. fendleri gene in transgenic plants of a fad2 mutant of Arabidopsis, which is deficient in cytoplasmic oleate delta 12 desaturase activity, resulted in partial suppression of the mutant phenotype in roots. Thus, unlike the hydroxylase from R. communis, the L. fendleri enzyme has both hydroxylase and desaturase activities. Fusion of the 5' flanking region of the LFAH12 gene to the beta-glucuronidase coding sequence resulted in a high level of early seed-specific expression of beta-glucuronidase activity in transgenic Arabidopsis plants. SN - 0960-7412 UR - https://www.unboundmedicine.com/medline/citation/9680976/A_bifunctional_oleate_12_hydroxylase:_desaturase_from_Lesquerella_fendleri_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0960-7412&date=1998&volume=13&issue=2&spage=201 DB - PRIME DP - Unbound Medicine ER -