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A distinct type of glycerol-3-phosphate acyltransferase with sn-2 preference and phosphatase activity producing 2-monoacylglycerol
- Source :
- Proceedings of the National Academy of Sciences of the United States of America, Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2010, 107 (26), pp.12040-12045. ⟨10.1073/pnas.0914149107⟩
- Publication Year :
- 2010
- Publisher :
- HAL CCSD, 2010.
-
Abstract
- The first step in assembly of membrane and storage glycerolipids is acylation of glycerol-3-phosphate (G3P). All previously characterized membrane-bound, eukaryotic G3P acyltransferases (GPATs) acylate the sn -1 position to produce lysophosphatidic acid (1-acyl-LPA). Cutin is a glycerolipid with omega-oxidized fatty acids and glycerol as integral components. It occurs as an extracellular polyester on the aerial surface of all plants, provides a barrier to pathogens and resistance to stress, and maintains organ identity. We have determined that Arabidopsis acyltransferases GPAT4 and GPAT6 required for cutin biosynthesis esterify acyl groups predominantly to the sn -2 position of G3P. In addition, these acyltransferases possess a phosphatase domain that results in sn -2 monoacylglycerol (2-MAG) rather than LPA as the major product. Such bifunctional activity has not been previously described in any organism. The possible roles of 2-MAGs as intermediates in cutin synthesis are discussed. GPAT5, which is essential for the accumulation of suberin aliphatics, also exhibits a strong preference for sn -2 acylation. However, phosphatase activity is absent and 2-acyl-LPA is the major product. Clearly, plant GPATs can catalyze more reactions than the sn -1 acylation by which they are currently categorized. Close homologs of GPAT4-6 are present in all land plants, but not in animals, fungi or microorganisms (including algae). Thus, these distinctive acyltransferases may have been important for evolution of extracellular glycerolipid polymers and adaptation of plants to a terrestrial environment. These results provide insight into the biosynthetic assembly of cutin and suberin, the two most abundant glycerolipid polymers in nature.
- Subjects :
- Models, Molecular
0106 biological sciences
Acylation
Membrane lipids
[SDV]Life Sciences [q-bio]
Molecular Sequence Data
Phosphatase
Arabidopsis
Saccharomyces cerevisiae
Cutin
Biology
Genes, Plant
01 natural sciences
Substrate Specificity
Evolution, Molecular
Membrane Lipids
03 medical and health sciences
chemistry.chemical_compound
Biosynthesis
Suberin
Amino Acid Sequence
Triticum
ComputingMilieux_MISCELLANEOUS
DNA Primers
030304 developmental biology
0303 health sciences
Multidisciplinary
Base Sequence
Sequence Homology, Amino Acid
Arabidopsis Proteins
food and beverages
Biological Sciences
Lipids
Recombinant Proteins
Monoacylglycerol lipase
Amino Acid Substitution
Biochemistry
chemistry
Acyltransferases
Glycerol-3-Phosphate O-Acyltransferase
Mutagenesis, Site-Directed
Monoglycerides
lipids (amino acids, peptides, and proteins)
Mutant Proteins
010606 plant biology & botany
Subjects
Details
- Language :
- English
- ISSN :
- 00278424 and 10916490
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America, Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2010, 107 (26), pp.12040-12045. ⟨10.1073/pnas.0914149107⟩
- Accession number :
- edsair.doi.dedup.....dd4535e22939549abce49754bae812ce