title: Arabidopsis thaliana T-DNA mutants implicate GAUT genes in the biosynthesis of pectin and xylan in cell walls and seed testa.
abstract: Galacturonosyltransferase 1 (GAUT1) is an alpha1,4-D-galacturonosyltransferase that transfers galacturonic acid from uridine 5'-diphosphogalacturonic acid onto the pectic polysaccharide homogalacturonan (Sterling et al., 2006). The 25-member Arabidopsis thaliana GAUT1-related gene family encodes 15 GAUT and 10 GAUT-like (GATL) proteins with, respectively, 56-84 and 42-53% amino acid sequence similarity to GAUT1. Previous phylogenetic analyses of AtGAUTs indicated three clades: A through C. A comparative phylogenetic analysis of the Arabidopsis, poplar and rice GAUT families has sub-classified the GAUTs into seven clades: clade A-1 (GAUTs 1 to 3); A-2 (GAUT4); A-3 (GAUTs 5 and 6); A-4 (GAUT7); B-1 (GAUTs 8 and 9); B-2 (GAUTs 10 and 11); and clade C (GAUTs 12 to 15). The Arabidopsis GAUTs have a distribution comparable to the poplar orthologs, with the exception of GAUT2, which is absent in poplar. Rice, however, has no orthologs of GAUTs 2 and 12 and has multiple apparent orthologs of GAUTs 1, 4, and 7 compared with either Arabidopsis or poplar. The cell wall glycosyl residue compositions of 26 homozygous T-DNA insertion mutants for 13 of 15 Arabidopsis GAUT genes reveal significantly and reproducibly different cell walls in specific tissues of gaut mutants 6, 8, 9, 10, 11, 12, 13, and 14 from that of wild-type Arabidopsis walls. Pectin and xylan polysaccharides are affected by the loss of GAUT function, as demonstrated by the altered galacturonic acid, xylose, rhamnose, galactose, and arabinose composition of distinct gaut mutant walls. The wall glycosyl residue compositional phenotypes observed among the gaut mutants suggest that at least six different biosynthetic linkages in pectins and/or xylans are affected by the lesions in these GAUT genes. Evidence is also presented to support a role for GAUT11 in seed mucilage expansion and in seed wall and mucilage composition.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
authors.forename: Kerry H
authors.initials: KH
authors.lastname: Caffall
authors.forename: Sivakumar
authors.initials: S
authors.lastname: Pattathil
authors.forename: Sarah E
authors.initials: SE
authors.lastname: Phillips
authors.forename: Michael G
authors.initials: MG
authors.lastname: Hahn
authors.forename: Debra
authors.initials: D
authors.lastname: Mohnen
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000145:classification / Q000235:genetics / Q000502:physiology*; D002473:Cell Wall / Q000235:genetics / Q000378:metabolism*; D004269:DNA, Bacterial / Q000235:genetics*; D008401:Gas Chromatography-Mass Spectrometry; D018506:Gene Expression Regulation, Plant / Q000235:genetics / Q000502:physiology; D005838:Genotype; D016695:Glycosyltransferases / Q000235:genetics / Q000378:metabolism; D012275:Oryza / Q000235:genetics; D010368:Pectins / Q000096:biosynthesis* / Q000235:genetics; D010802:Phylogeny; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D032107:Populus / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012639:Seeds / Q000235:genetics / Q000378:metabolism*; D014990:Xylans / Q000096:biosynthesis* / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; D004269:DNA, Bacterial; C036483:T-DNA; D014990:Xylans; D010368:Pectins; D016695:Glycosyltransferases