Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum

Salim Al-Babili; Philippe Hugueney; Michael Schledz; Ralf Welsch; Hanns Frohnmeyer; Oliver Laule; Peter Beyer

doi:10.1016/S0014-5793(00)02193-1

Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum

Salim Al-Babili, Philippe Hugueney, Michael Schledz, Ralf Welsch, Hanns Frohnmeyer, Oliver Laule, Peter Beyer^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

88 Scopus citations

Abstract

The polymerase chain reaction analysis of potato plants, transformed with capsanthin capsorubin synthase ccs, revealed the presence of a highly related gene. The cloned cDNA showed at the protein level 89.6% identity to CCS. This suggested that the novel enzyme catalyzes a mechanistically similar reaction. Such a reaction is represented by neoxanthin synthase (NXS), forming the xanthophyll neoxanthin, a direct substrate for abscisic acid formation. The function of the novel enzyme could be proven by transient expression in plant protoplasts and high performance liquid chromatography analysis. The cloned NXS was imported in vitro into plastids, the compartment of carotenoid biosynthesis. (C) 2000 Federation of European Biochemical Societies.

Original language	English (US)
Pages (from-to)	168-172
Number of pages	5
Journal	FEBS Letters
Volume	485
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(00)02193-1
State	Published - Nov 24 2000
Externally published	Yes

Keywords

Abscisic acid
Capsanthin capsorubin synthase
Carotenoid
Neoxanthin synthase
Violaxanthin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(00)02193-1

Cite this

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title = "Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum",

abstract = "The polymerase chain reaction analysis of potato plants, transformed with capsanthin capsorubin synthase ccs, revealed the presence of a highly related gene. The cloned cDNA showed at the protein level 89.6% identity to CCS. This suggested that the novel enzyme catalyzes a mechanistically similar reaction. Such a reaction is represented by neoxanthin synthase (NXS), forming the xanthophyll neoxanthin, a direct substrate for abscisic acid formation. The function of the novel enzyme could be proven by transient expression in plant protoplasts and high performance liquid chromatography analysis. The cloned NXS was imported in vitro into plastids, the compartment of carotenoid biosynthesis. (C) 2000 Federation of European Biochemical Societies.",

keywords = "Abscisic acid, Capsanthin capsorubin synthase, Carotenoid, Neoxanthin synthase, Violaxanthin",

author = "Salim Al-Babili and Philippe Hugueney and Michael Schledz and Ralf Welsch and Hanns Frohnmeyer and Oliver Laule and Peter Beyer",

year = "2000",

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doi = "10.1016/S0014-5793(00)02193-1",

language = "English (US)",

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journal = "FEBS Letters",

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TY - JOUR

T1 - Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum

AU - Al-Babili, Salim

AU - Hugueney, Philippe

AU - Schledz, Michael

AU - Welsch, Ralf

AU - Frohnmeyer, Hanns

AU - Laule, Oliver

AU - Beyer, Peter

PY - 2000/11/24

Y1 - 2000/11/24

N2 - The polymerase chain reaction analysis of potato plants, transformed with capsanthin capsorubin synthase ccs, revealed the presence of a highly related gene. The cloned cDNA showed at the protein level 89.6% identity to CCS. This suggested that the novel enzyme catalyzes a mechanistically similar reaction. Such a reaction is represented by neoxanthin synthase (NXS), forming the xanthophyll neoxanthin, a direct substrate for abscisic acid formation. The function of the novel enzyme could be proven by transient expression in plant protoplasts and high performance liquid chromatography analysis. The cloned NXS was imported in vitro into plastids, the compartment of carotenoid biosynthesis. (C) 2000 Federation of European Biochemical Societies.

AB - The polymerase chain reaction analysis of potato plants, transformed with capsanthin capsorubin synthase ccs, revealed the presence of a highly related gene. The cloned cDNA showed at the protein level 89.6% identity to CCS. This suggested that the novel enzyme catalyzes a mechanistically similar reaction. Such a reaction is represented by neoxanthin synthase (NXS), forming the xanthophyll neoxanthin, a direct substrate for abscisic acid formation. The function of the novel enzyme could be proven by transient expression in plant protoplasts and high performance liquid chromatography analysis. The cloned NXS was imported in vitro into plastids, the compartment of carotenoid biosynthesis. (C) 2000 Federation of European Biochemical Societies.

KW - Abscisic acid

KW - Capsanthin capsorubin synthase

KW - Carotenoid

KW - Neoxanthin synthase

KW - Violaxanthin

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DO - 10.1016/S0014-5793(00)02193-1

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AN - SCOPUS:0034711455

SN - 0014-5793

VL - 485

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JO - FEBS Letters

JF - FEBS Letters

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ER -

Identification of a novel gene coding for neoxanthin synthase from Solanum tuberosum

Abstract

Keywords

ASJC Scopus subject areas

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