2012
DOI: 10.1074/jbc.m111.311571
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Characterization of Galacturonosyl Transferase Genes rgtA, rgtB, rgtC, rgtD, and rgtE Responsible for Lipopolysaccharide Synthesis in Nitrogen-fixing Endosymbiont Rhizobium leguminosarum

Abstract: Background: Rhizobium LPS has four GalA residues. Results: RgtDE add GalA to the lipid A and synthesize Dod-P-GalA. RgtABCDE mutants are affected in DOC and PmxB sensitivity. Conclusion: Sequence of GalA addition to LPS is RgtDABC. Lipid A GalA provides membrane stability and PmxB resistance. Significance: GalA negative charges are required for membrane stability and implicated for interaction with plant host antimicrobial peptides.

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Cited by 9 publications
(13 citation statements)
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“…A chitinase-like protein was overexpressed in the Arabidopsis hot2 mutant, which has excellent tolerance to heat, salt, and drought stresses [32]. Galacturonosyl transferase is the core element of pectin biosynthesis in the plant cell wall, indicating that upregulation of alpha-1,4-galacturonosyltransferase could adjust the osmotic potential via alterations to the plant cell wall [33]. Significant upregulation of genes encoding beta-amylase, which are involved in starch and sucrose metabolism (ko00500) was also noted.…”
Section: Discussionmentioning
confidence: 99%
“…A chitinase-like protein was overexpressed in the Arabidopsis hot2 mutant, which has excellent tolerance to heat, salt, and drought stresses [32]. Galacturonosyl transferase is the core element of pectin biosynthesis in the plant cell wall, indicating that upregulation of alpha-1,4-galacturonosyltransferase could adjust the osmotic potential via alterations to the plant cell wall [33]. Significant upregulation of genes encoding beta-amylase, which are involved in starch and sucrose metabolism (ko00500) was also noted.…”
Section: Discussionmentioning
confidence: 99%
“…Despite the apparent up-regulation of PagL in R. etli bacteroids, the modification catalyzed by PagL does not appear to be essential for nodule development and nitrogen-fixation. The 3- O deacylation reaction, like other lipid A modification reactions, could play a role in protecting bacterial symbionts from the plant immune response during pathogenic infections [18, 36, 48]. PagL activity in Gram-negative pathogens has been linked to an increase in resistance to antimicrobial peptides [49].…”
Section: Discussionmentioning
confidence: 99%
“…The resulting lipid A intermediate, Kdo 2 -lipid IV A intermediate is then processed by enzymes that are absent in E. coli . The R. etli lipid A modification enzymes include a 4′-phosphatase (LpxF) [12], a 1-phosphatase (LpxE) [13], a C28-specific long-chain acyltransferase (LpxXL) [14, 15], a galacturonosyltransferase (RgtD) [1618], a lipid A oxidase (LpxQ) [19, 20], and an unidentified 3- O -deacylase [21]. …”
Section: Introductionmentioning
confidence: 99%
“…In Rhizobia, the phosphatases LpxE and LpxF dephosphorylate the 1 and 4 positions, respectively, of lipid A at the periplasmic surface of the IM (Karbarz et al, 2003;Wang et al, 2006). Sugars are then added to the 1 and 4 positions by the glycosyltransferases RgtF and RgtD, respectively, before the transport of mature LPS molecules to the OM (Brown et al, 2012(Brown et al, , 2013. NA1000 harbors a gene (CCNA_03113) with similarity to LpxE, but none with similarity to LpxF, raising the possibility that CtpA substitutes for LpxF.…”
Section: Ctpa Is Required For Wild-type Lipid a Structure And Abundancementioning
confidence: 99%