Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus

Li Tian, Dean Dellapenna

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

Xanthophylls are oxygenated carotenoids that perform critical roles in plants. β-carotene hydroxylases (β-hydroxylases) add hydroxyl groups to the β-rings of carotenes and have been cloned from several bacteria and plants, including Arabidopsis. The lut1 mutation of Arabidopsis disrupts ε-ring hydroxylation and has been suggested to identify a related carotene hydroxylase that functions specifically on ε-ring structures. We have used library screening and genomics-based approaches to isolate a second β-hydroxylase genomic clone and its corresponding cDNA from Arabidopsis. The encoded protein is 70% identical to the previously reported Arabidopsis β-hydroxylase 1. Phylogenetic analysis indicates a common origin for the two proteins, however, their different chromosomal locations, intron positions and intron sizes suggest their duplication is not recent. Although both hydroxylases are expressed in all Arabidopsis tissues analyzed, β-hydroxylase 1 mRNA is always present at higher levels. Both cDNAs encode proteins that efficiently hydroxylate the C-3 position of β-ring containing carotenes and are only weakly active towards ε-ring containing carotenes. Neither β-hydroxylase cDNA maps to the LUT1 locus, and the genomic region encompassing the LUT1 locus does not contain a third related hydroxylase. These data indicate that the LUT1 locus encodes a protein necessary for ε-ring hydroxylation but unrelated to β-hydroxylases at the level of amino acid sequence.

Original languageEnglish (US)
Pages (from-to)379-388
Number of pages10
JournalPlant Molecular Biology
Volume47
Issue number3
DOIs
StatePublished - 2001
Externally publishedYes

Fingerprint

Carotenoids
carotenes
Mixed Function Oxygenases
Arabidopsis
carotenoids
Genes
loci
hydroxylation
genomics
genes
introns
proteins
Hydroxylation
Complementary DNA
xanthophylls
Introns
Proteins
Xanthophylls
amino acid sequences
clones

Keywords

  • Arabidopsis
  • Carotenoid
  • Hydroxylase
  • lut1
  • TaqMan
  • Xanthophyll

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus. / Tian, Li; Dellapenna, Dean.

In: Plant Molecular Biology, Vol. 47, No. 3, 2001, p. 379-388.

Research output: Contribution to journalArticle

@article{b30a87f25c484196aaa2e7d57d6d7c4a,
title = "Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus",
abstract = "Xanthophylls are oxygenated carotenoids that perform critical roles in plants. β-carotene hydroxylases (β-hydroxylases) add hydroxyl groups to the β-rings of carotenes and have been cloned from several bacteria and plants, including Arabidopsis. The lut1 mutation of Arabidopsis disrupts ε-ring hydroxylation and has been suggested to identify a related carotene hydroxylase that functions specifically on ε-ring structures. We have used library screening and genomics-based approaches to isolate a second β-hydroxylase genomic clone and its corresponding cDNA from Arabidopsis. The encoded protein is 70{\%} identical to the previously reported Arabidopsis β-hydroxylase 1. Phylogenetic analysis indicates a common origin for the two proteins, however, their different chromosomal locations, intron positions and intron sizes suggest their duplication is not recent. Although both hydroxylases are expressed in all Arabidopsis tissues analyzed, β-hydroxylase 1 mRNA is always present at higher levels. Both cDNAs encode proteins that efficiently hydroxylate the C-3 position of β-ring containing carotenes and are only weakly active towards ε-ring containing carotenes. Neither β-hydroxylase cDNA maps to the LUT1 locus, and the genomic region encompassing the LUT1 locus does not contain a third related hydroxylase. These data indicate that the LUT1 locus encodes a protein necessary for ε-ring hydroxylation but unrelated to β-hydroxylases at the level of amino acid sequence.",
keywords = "Arabidopsis, Carotenoid, Hydroxylase, lut1, TaqMan, Xanthophyll",
author = "Li Tian and Dean Dellapenna",
year = "2001",
doi = "10.1023/A:1011623907959",
language = "English (US)",
volume = "47",
pages = "379--388",
journal = "Plant Molecular Biology",
issn = "0167-4412",
publisher = "Springer Netherlands",
number = "3",

}

TY - JOUR

T1 - Characterization of a second carotenoid β-hydroxylase gene from Arabidopsis and its relationship to the LUT1 locus

AU - Tian, Li

AU - Dellapenna, Dean

PY - 2001

Y1 - 2001

N2 - Xanthophylls are oxygenated carotenoids that perform critical roles in plants. β-carotene hydroxylases (β-hydroxylases) add hydroxyl groups to the β-rings of carotenes and have been cloned from several bacteria and plants, including Arabidopsis. The lut1 mutation of Arabidopsis disrupts ε-ring hydroxylation and has been suggested to identify a related carotene hydroxylase that functions specifically on ε-ring structures. We have used library screening and genomics-based approaches to isolate a second β-hydroxylase genomic clone and its corresponding cDNA from Arabidopsis. The encoded protein is 70% identical to the previously reported Arabidopsis β-hydroxylase 1. Phylogenetic analysis indicates a common origin for the two proteins, however, their different chromosomal locations, intron positions and intron sizes suggest their duplication is not recent. Although both hydroxylases are expressed in all Arabidopsis tissues analyzed, β-hydroxylase 1 mRNA is always present at higher levels. Both cDNAs encode proteins that efficiently hydroxylate the C-3 position of β-ring containing carotenes and are only weakly active towards ε-ring containing carotenes. Neither β-hydroxylase cDNA maps to the LUT1 locus, and the genomic region encompassing the LUT1 locus does not contain a third related hydroxylase. These data indicate that the LUT1 locus encodes a protein necessary for ε-ring hydroxylation but unrelated to β-hydroxylases at the level of amino acid sequence.

AB - Xanthophylls are oxygenated carotenoids that perform critical roles in plants. β-carotene hydroxylases (β-hydroxylases) add hydroxyl groups to the β-rings of carotenes and have been cloned from several bacteria and plants, including Arabidopsis. The lut1 mutation of Arabidopsis disrupts ε-ring hydroxylation and has been suggested to identify a related carotene hydroxylase that functions specifically on ε-ring structures. We have used library screening and genomics-based approaches to isolate a second β-hydroxylase genomic clone and its corresponding cDNA from Arabidopsis. The encoded protein is 70% identical to the previously reported Arabidopsis β-hydroxylase 1. Phylogenetic analysis indicates a common origin for the two proteins, however, their different chromosomal locations, intron positions and intron sizes suggest their duplication is not recent. Although both hydroxylases are expressed in all Arabidopsis tissues analyzed, β-hydroxylase 1 mRNA is always present at higher levels. Both cDNAs encode proteins that efficiently hydroxylate the C-3 position of β-ring containing carotenes and are only weakly active towards ε-ring containing carotenes. Neither β-hydroxylase cDNA maps to the LUT1 locus, and the genomic region encompassing the LUT1 locus does not contain a third related hydroxylase. These data indicate that the LUT1 locus encodes a protein necessary for ε-ring hydroxylation but unrelated to β-hydroxylases at the level of amino acid sequence.

KW - Arabidopsis

KW - Carotenoid

KW - Hydroxylase

KW - lut1

KW - TaqMan

KW - Xanthophyll

UR - http://www.scopus.com/inward/record.url?scp=0034813551&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034813551&partnerID=8YFLogxK

U2 - 10.1023/A:1011623907959

DO - 10.1023/A:1011623907959

M3 - Article

C2 - 11587509

AN - SCOPUS:0034813551

VL - 47

SP - 379

EP - 388

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 3

ER -