A new Acyi-CoA Synthetase, Located in Higher Plant Cytosol

Gerbling, Heidrun; Axiotis, Stella; Douce, Roland

doi:10.1016/s0176-1617(11)81824-9

Cited by 8 publications

(2 citation statements)

References 13 publications

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“…In plants, FAs are activated by acyl-CoA synthetase and converted into acyl-CoA esters ( Gerbling et al, 1994 ). ACBPs have been suggested to maintain the acyl-CoA pools in plants ( Yurchenko et al, 2009 ).…”

Section: Introductionmentioning

confidence: 99%

Depletion of Arabidopsis ACYL-COA-BINDING PROTEIN3 Affects Fatty Acid Composition in the Phloem

Lung

et al. 2018

Front. Plant Sci.

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Oxylipins are crucial components in plant wound responses that are mobilised via the plant vasculature. Previous studies have shown that the overexpression of an Arabidopsis acyl-CoA-binding protein, AtACBP3, led to an accumulation of oxylipin-containing galactolipids, and AtACBP3pro::BETA-GLUCURONIDASE (GUS) was expressed in the phloem of transgenic Arabidopsis. To investigate the role of AtACBP3 in the phloem, reverse transcription-polymerase chain reaction and western blot analysis of phloem exudates from the acbp3 mutant and wild type revealed that the AtACBP3 protein, but not its mRNA, was detected in the phloem sap. Furthermore, micrografting demonstrated that AtACBP3 expressed from the 35S promoter was translocated from shoot to root. Subsequently, AtACBP3 was localised to the companion cells, sieve elements and the apoplastic space of phloem tissue by immunogold electron microscopy using anti-AtACBP3 antibodies. AtACBP3pro::GUS was induced locally in Arabidopsis leaves upon wounding, and the expression of wound-responsive jasmonic acid marker genes (JASMONATE ZIM-DOMAIN10, VEGETATIVE STORAGE PROTEIN2, and LIPOXYGENASE2) increased more significantly in both locally wounded and systemic leaves of the wild type in comparison to acbp3 and AtACBP3-RNAi. Oxylipin-related fatty acid (FA) (C18:2-FA, C18:3-FA and methyl jasmonate) content was observed to be lower in acbp3 and AtACBP3-RNAi than wild-type phloem exudates using gas chromatography-mass spectrometry. Experiments using recombinant AtACBP3 in isothermal titration calorimetry analysis showed that medium- and long-chain acyl-CoA esters bind (His)6-AtACBP3 with KD values in the micromolar range. Taken together, these results suggest that AtACBP3 is likely to be a phloem-mobile protein that affects the FA pool and jasmonate content in the phloem, possibly by its binding to acyl-CoA esters.

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Section: Introductionmentioning

confidence: 99%

Depletion of Arabidopsis ACYL-COA-BINDING PROTEIN3 Affects Fatty Acid Composition in the Phloem

Lung

et al. 2018

Front. Plant Sci.

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“…Indeed, analysis of the primary sequence of the Arabidopsis biotin synthase by the PSORT algorithm (Nakai and Kanehisa, 1992) predicts that this protein is targeted to mitochondria. Although the primary sequence of the Arabidopsis biotin synthase predicts that the enzyme may be present in an organelle, possibly the mitochondrion, this will need to be shown directly, particularly in light of the fact that most of the free biotin in mesophyll cells of leaves has been shown to be in the cytosol (Baldet et al, 1993a) and that a pimeloyl-COA synthetase that may be involved in biotin biosynthesis has been shown to be in the cytosol (Gerbling et al, 1994). If biotin synthase is located in an organelle, then organellesynthesized biotin would need to be exported to accumulate in the cytosol.…”

Section: Primary Structure Of Biotin Synthasementioning

confidence: 99%

Characterization of the cDNA and Gene Coding for the Biotin Synthase of Arabidopsis thaliana

Weaver

Wurtele

et al. 1996

Plant Physiol.

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Biotin, an essential cofactor, is synthesized de novo only by plants and some microbes. An Arabidopsis thaliana expressed sequence tag that shows sequence similarity to the carboxyl end of biotin synthase from Escherichia coli was used to isolate a near-fulllength cDNA. This cDNA was shown to code for the Arabidopsis biotin synthase by its ability to complement a bioB mutant of E. coli.Site-specific mutagenesis indicates that residue threonine-173, which is highly conserved in biotin synthases, is important for catalytic competence of the enzyme. The primary sequence of the Arabidopsis biotin synthase is most similar to biotin synthases from E. coli, Serratia marcescens, and Saccharomyces cerevisiae (about 50% sequence identity) and more distantly related to the Bacillus sphaericus enzyme (33% sequence identity). The primary sequence of the amino terminus of the Arabidopsis biotin synthase may represent an organelle-targeting transit peptide. The single Arabidopsis gene coding for biotin synthase, 9/02, was isolated and sequenced. The biotin synthase coding sequence i s interrupted by five introns. The gene sequence upstream of the translation start site has severa1 unusual features, including imperfect palindromes and polypyrimidine sequences, which may function in the transcriptional regulation of the 9\02 gene.

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Molecular Biology, Enzymology, and Physiology of β-Oxidation

Hooks

2002

Plant Peroxisomes

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A new Acyi-CoA Synthetase, Located in Higher Plant Cytosol

Cited by 8 publications

References 13 publications

Depletion of Arabidopsis ACYL-COA-BINDING PROTEIN3 Affects Fatty Acid Composition in the Phloem

Depletion of Arabidopsis ACYL-COA-BINDING PROTEIN3 Affects Fatty Acid Composition in the Phloem

Characterization of the cDNA and Gene Coding for the Biotin Synthase of Arabidopsis thaliana

Molecular Biology, Enzymology, and Physiology of β-Oxidation

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