دورية أكاديمية
أعرض في EDS

Molecular characterization of an Arabidopsis acyl-coenzyme a synthetase localized on glyoxysomal membranes.

التفاصيل البيبلوغرافية
العنوان: Molecular characterization of an Arabidopsis acyl-coenzyme a synthetase localized on glyoxysomal membranes.
المؤلفون: Hayashi H; Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan., De Bellis L, Hayashi Y, Nito K, Kato A, Hayashi M, Hara-Nishimura I, Nishimura M
المصدر: Plant physiology [Plant Physiol] 2002 Dec; Vol. 130 (4), pp. 2019-26.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Society of Plant Biologists Country of Publication: United States NLM ID: 0401224 Publication Model: Print Cited Medium: Print ISSN: 0032-0889 (Print) Linking ISSN: 00320889 NLM ISO Abbreviation: Plant Physiol Subsets: MEDLINE
أسماء مطبوعة: Publication: : [Rockville, MD] : American Society of Plant Biologists
Original Publication: Lancaster, Pa., American Society of Plant Physiologists.
مواضيع طبية MeSH: Arabidopsis/*genetics , Arabidopsis Proteins/*genetics , Coenzyme A Ligases/*genetics , Glyoxysomes/*enzymology , Intracellular Membranes/*enzymology, Amino Acid Sequence ; Arabidopsis/enzymology ; Arabidopsis/growth & development ; Arabidopsis Proteins/isolation & purification ; Arabidopsis Proteins/metabolism ; Cloning, Molecular ; Coenzyme A Ligases/isolation & purification ; Coenzyme A Ligases/metabolism ; DNA, Complementary/chemistry ; DNA, Complementary/genetics ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Plant ; Germination/genetics ; Glyoxysomes/ultrastructure ; Immunoblotting ; Intracellular Membranes/ultrastructure ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Seeds/enzymology ; Seeds/genetics ; Seeds/growth & development ; Sequence Analysis, DNA
مستخلص: In higher plants, fat-storing seeds utilize storage lipids as a source of energy during germination. To enter the beta-oxidation pathway, fatty acids need to be activated to acyl-coenzyme As (CoAs) by the enzyme acyl-CoA synthetase (ACS; EC 6.2.1.3). Here, we report the characterization of an Arabidopsis cDNA clone encoding for a glyoxysomal acyl-CoA synthetase designated AtLACS6. The cDNA sequence is 2,106 bp long and it encodes a polypeptide of 701 amino acids with a calculated molecular mass of 76,617 D. Analysis of the amino-terminal sequence indicates that acyl-CoA synthetase is synthesized as a larger precursor containing a cleavable amino-terminal presequence so that the mature polypeptide size is 663 amino acids. The presequence shows high similarity to the typical PTS2 (peroxisomal targeting signal 2). The AtLACS6 also shows high amino acid identity to prokaryotic and eukaryotic fatty acyl-CoA synthetases. Immunocytochemical and cell fractionation analyses indicated that the AtLACS6 is localized on glyoxysomal membranes. AtLACS6 was overexpressed in insect cells and purified to near homogeneity. The purified enzyme is particularly active on long-chain fatty acids (C16:0). Results from immunoblot analysis revealed that the expression of both AtLACS6 and beta-oxidation enzymes coincide with fatty acid degradation. These data suggested that AtLACS6 might play a regulatory role both in fatty acid import into glyoxysomes by making a complex with other factors, e.g. PMP70, and in fatty acid beta-oxidation activating the fatty acids.
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سلسلة جزيئية: GENBANK AB030317
المشرفين على المادة: 0 (Arabidopsis Proteins)
0 (DNA, Complementary)
EC 6.2.1.- (Coenzyme A Ligases)
EC 6.2.1.3 (LACS6 protein, Arabidopsis)
تواريخ الأحداث: Date Created: 20021214 Date Completed: 20030530 Latest Revision: 20181113
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC166713
DOI: 10.1104/pp.012955
PMID: 12481085
قاعدة البيانات: MEDLINE
الوصف
تدمد:0032-0889
DOI:10.1104/pp.012955