Literature summary for 4.2.1.134 extracted from

Morineau, C.; Gissot, L.; Bellec, Y.; Hematy, K.; Tellier, F.; Renne, C.; Haslam, R.; Beaudoin, F.; Napier, J.; Faure, J.D.
Dual fatty acid elongase complex interactions in Arabidopsis (2016), PLoS ONE, 11, e0160631 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene MTH12.2 or At5g59770, expression analysis, PTPLA is fused with CYFP- or NYFP- at the N-terminal of the protein prevent potential interference with ER retention signal located at the C-terminal end, transient expression of 35S:mCherry-PTPLA constructs in Nicotiana benthamiana. The subcellular distribution of mCherry-PTPLA shows the characteristic endoplasmic reticulum network which is confirmed by its colocalization with endoplasmic reticulum-localized GFP-PAS2 fusion, in contrary to the PTPLA promoter, the KCR2 promoter is also expressed in cotyledons, leaves and in the meristem of secondary roots	Arabidopsis thaliana
gene PAS2 or At5g10480, expression analysis, transient expression of GFP-PAS2 fusion constructs in Nicotiana benthamiana endoplasmic reticulum	Arabidopsis thaliana

Cloned (Comment)

Organism

gene MTH12.2 or At5g59770, expression analysis, PTPLA is fused with CYFP- or NYFP- at the N-terminal of the protein prevent potential interference with ER retention signal located at the C-terminal end, transient expression of 35S:mCherry-PTPLA constructs in Nicotiana benthamiana. The subcellular distribution of mCherry-PTPLA shows the characteristic endoplasmic reticulum network which is confirmed by its colocalization with endoplasmic reticulum-localized GFP-PAS2 fusion, in contrary to the PTPLA promoter, the KCR2 promoter is also expressed in cotyledons, leaves and in the meristem of secondary roots

Arabidopsis thaliana

gene PAS2 or At5g10480, expression analysis, transient expression of GFP-PAS2 fusion constructs in Nicotiana benthamiana endoplasmic reticulum

Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	enzyme PTPLA associates with the elongase complex in the endoplasmic reticulum and interacts with the elongase complex subunits	Arabidopsis thaliana	5783	-

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q8GW27	-	-
Arabidopsis thaliana	Q8VZB2	-	-
Saccharomyces cerevisiae	P40857	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cotyledon	-	Arabidopsis thaliana	-
endodermis	-	Arabidopsis thaliana	-
leaf	-	Arabidopsis thaliana	-
additional information	enzyme expression analysis, pPAS2:GUS staining is present in mature roots and secondary roots but also expressed in the epidermis of cotyledons and leaves. In mature primary roots, pPAS2:GUS expression profile is specific to the endodermis	Arabidopsis thaliana	-
additional information	enzyme expression analysis, pPTPLA:GUS staining is specifically localized in mature primary and secondary roots and restricted to the central cylinder. In mature primary roots pPTPLA:GUS appears to be restricted to vascular tissue	Arabidopsis thaliana	-
root	-	Arabidopsis thaliana	-
vascular tissue	enzyme PTPLA is specifically expressed in root vascular tissues	Arabidopsis thaliana	-

Synonyms

Synonyms	Comment	Organism
3 hydroxyacyl-CoA dehydratase	-	Arabidopsis thaliana
3 hydroxyacyl-CoA dehydratase	-	Saccharomyces cerevisiae
3-hydroxyacyl-CoA dehydratase	-	Arabidopsis thaliana
3-hydroxyacyl-CoA dehydratase	-	Saccharomyces cerevisiae
Fatty acid elongase	-	Arabidopsis thaliana
Fatty acid elongase	-	Saccharomyces cerevisiae
HCD	-	Arabidopsis thaliana
HCD	-	Saccharomyces cerevisiae
PAS2	-	Arabidopsis thaliana
PASTICCINO 2	-	Arabidopsis thaliana
PHS1	-	Saccharomyces cerevisiae
PTPLA	-	Arabidopsis thaliana
PTPLA dehydratase	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
evolution	the very-long-chain 3-hydroxyacyl-CoA dehydratase PTPLA sequence is as divergent from very-long-chain 3-hydroxyacyl-CoA dehydratase PAS2 sequence as it is from yeast very-long-chain 3-hydroxyacyl-CoA dehydratase PHS1	Arabidopsis thaliana
malfunction	loss of function of the elongase 3 hydroxyacyl-CoA dehydratase PHS1 in yeast prevents growth and induces cytokinesis defects. Protein tyrosine phosphatase-like (PTPLA) is able to restore yeast phs1 growth and very long chain fatty acids (VLCFAs) elongation, phenotype of the PTPLA complementation of Tet-PHS1 mutant. The absence of the dehydratase PHS1 blocks fatty acid elongation and leads to reduced VLCFA levels in yeast. As a corollary, phytosphingosine (PHS) level is enhanced since VLCFA are required for sphingolipids synthesis. PTPLA expression in Tet-PHS1+DOX is able to reduce PHS levels and induce VLCFA elongation to wild-type levels. The hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs	Saccharomyces cerevisiae
malfunction	the hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs	Arabidopsis thaliana
malfunction	the hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs. Loss of function of the elongase 3 hydroxyacyl-CoA dehydratase PASTICCINO2 (pas2-1) in plants prevents growth and induces cytokinesis defects. The disruption of VLCFA elongation in pas2-1 mutant induces cell proliferation and abnormal cytokinesis leading to defective differentiation in the apical part and shorter primary root. These developmental defects were linked with reduced VLCFA levels in triglycerides, waxes, sphingolipids and phospholipids. Moreover, the complete loss of PAS2 function is embryo lethal. Protein tyrosine phosphatase-like (PTPLA) is not able to restore the plant pas2-1 defects. The lack of complementation of a null allele of yeast phs1 could be caused by some plant specific determinants of PTPLA activity	Arabidopsis thaliana
physiological function	comparative ectopic expression of the two very-long-chain 3-hydroxyacyl-CoA dehydratases PTPLA and PAS2 in their respective domains confirms the existence of two independent elongase complexes based on PAS2 or PTPLA dehydratase that are functionally interacting. The two dehydratases have specific expression profiles in the root with PAS2 mostly restricted to the endodermis, while PTPLA is confined in the vascular tissue and pericycle cells	Arabidopsis thaliana
physiological function	comparative ectopic expression of the two very-long-chain 3-hydroxyacyl-CoA dehydratases PTPLA and PAS2 in their respective domains confirms the existence of two independent elongase complexes based on PAS2 or PTPLA dehydratase that are functionally interacting. The two dehydratases have specific expression profiles in the root with PAS2 mostly restricted to the endodermis, while PTPLA is confined in the vascular tissue and pericycle cells. Protein tyrosine phosphatase-like (PTPLA), previously characterized as an inactive dehydratase, is not able to restore the plant pas2-1 defects. Enzyme PTPLA associates with the elongase complex in the endoplasmic reticulum. The specific elongase activity in vascular tissues regulates endodermal VLCFA elongation	Arabidopsis thaliana
physiological function	PTPLA expression induces fatty acid elongation in yeast Tet-PHS1 in presence of DOX and in wild-type strain	Saccharomyces cerevisiae