Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2007-11-16
pubmed:abstractText
Cutin and suberin are the two major lipid-based polymers of plants. Cutin is the structural polymer of the epidermal cuticle, the waterproof layer covering primary aerial organs and which is often the structure first encountered by phytopathogens. Suberin contributes to the control of diffusion of water and solutes across internal root tissues and in periderms. The enzymes responsible for assembly of the cutin polymer are largely unknown. We have identified two Arabidopsis acyltransferases essential for cutin biosynthesis, glycerol-3-phosphate acyltransferase (GPAT) 4 and GPAT8. Double knockouts gpat4/gpat8 were strongly reduced in cutin and were less resistant to desiccation and to infection by the fungus Alternaria brassicicola. They also showed striking defects in stomata structure including a lack of cuticular ledges between guard cells, highlighting the importance of cutin in stomatal biology. Overexpression of GPAT4 or GPAT8 in Arabidopsis increased the content of C16 and C18 cutin monomers in leaves and stems by 80%. In order to modify cutin composition, the acyltransferase GPAT5 and the cytochrome P450-dependent fatty acyl oxidase CYP86A1, two enzymes associated with suberin biosynthesis, were overexpressed. When both enzymes were overexpressed together the epidermal polyesters accumulated new C20 and C22 omega-hydroxyacids and alpha,omega-diacids typical of suberin, and the fine structure and water-barrier function of the cuticle were altered. These results identify GPATs as partners of fatty acyl oxidases in lipid polyester synthesis and indicate that their cooverexpression provides a strategy to probe the role of cutin composition and quantity in the function of plant cuticles.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-11217409, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-11493698, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-12169316, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-12805591, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-12893945, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-12897259, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-14532054, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-14675439, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-14973169, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-15241470, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-15247097, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-15375207, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-15584957, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-15806101, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16289150, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16299169, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16580871, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16600316, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16658054, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16820397, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-16959575, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17055542, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17210910, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17259262, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17351057, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17396154, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17427946, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17434790, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17449808, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-17496107, http://linkedlifedata.com/resource/pubmed/commentcorrection/17991776-9500987
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1091-6490
pubmed:author
pubmed:issnType
Electronic
pubmed:day
13
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18339-44
pubmed:dateRevised
2010-9-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Identification of acyltransferases required for cutin biosynthesis and production of cutin with suberin-like monomers.
pubmed:affiliation
Department of Plant Biology and Plant Research Laboratory, Department of Energy, Michigan State University, East Lansing, MI 48824, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.