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NodS is a 5-adenosyl-L-methionine-dependent methyltransferase that methylates chitooligosaccharides deacetylated at the nonreducing end

Danny Geelen UGent, Barbara Leyman UGent, Peter Mergaert UGent, Klaus Klarskov UGent, Marc Van Montagu UGent, Roberto Geremia UGent and Marcella Holsters UGent (1995) MOLECULAR MICROBIOLOGY. 17(2). p.387-397
abstract
In response to phenolic compounds exuded by the host plant, symbiotic Rhizobium bacteria produce signal molecules (Nod factors), consisting of lipochitooligosaccharides with strain-specific substitutions. In Azorhizobium caulinodans strain ORS571 these modifications are an O-arabinosyl group, an O-carbamoyl group, and an IV-methyl group. Several lines of evidence indicate that the nodS gene located in the nodABCSUIJ operon is implicated in the methylation of Nod factors, Previously we have shown that NodS is an S-adenosyl-L-methionine (SAM)-binding protein, essential for the L-[H-3-methyl]-methionine labelling of ORS571 Nod factors in vivo. Here, we present an in vitro assay showing that NodS from either A. caulinodans or Rhizobium species NGR234 methylates end-deacetylated chitooligosaccharides, using [H-3-methyl]-SAM as a methyl donor. The enzymatic and SAM-binding activity were correlated with the nodS gene and localized within the soluble protein fraction. The A. caulinodans nodS gene was expressed in Escherichia coil and a glutathione-S-transferase-NodS fusion protein purified. This protein bound SAM and could methylate end-deacetylated chitooligosaccharides, but could not fully methylate acetylated chitooligosaccharides or unmethylated lipo-chitooligosaccharides. These data implicate that the methylation step in the biosynthesis pathway of ORS571 Nod factors occurs after deacetylation and prior to acylation of the chitooligosaccharides.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
SESBANIA-ROSTRATA, NODULATION SIGNALS, STRAIN NGR234, BRADYRHIZOBIUM-JAPONICUM, AZORHIZOBIUM-CAULINODANS, LIPO-OLIGOSACCHARIDE SIGNALS, RHIZOBIUM-MELILOTI, HOST SPECIFICITY, GENES, IDENTIFICATION
journal title
MOLECULAR MICROBIOLOGY
Mol. Microbiol.
volume
17
issue
2
pages
387 - 397
Web of Science type
Article
ISSN
0950-382X
DOI
10.1111/j.1365-2958.1995.mmi_17020387.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
195165
handle
http://hdl.handle.net/1854/LU-195165
date created
2004-01-14 13:42:00
date last changed
2013-11-06 15:53:28
@article{195165,
  abstract     = {In response to phenolic compounds exuded by the host plant, symbiotic Rhizobium bacteria produce signal molecules (Nod factors), consisting of lipochitooligosaccharides with strain-specific substitutions. In Azorhizobium caulinodans strain ORS571 these modifications are an O-arabinosyl group, an O-carbamoyl group, and an IV-methyl group. Several lines of evidence indicate that the nodS gene located in the nodABCSUIJ operon is implicated in the methylation of Nod factors, Previously we have shown that NodS is an S-adenosyl-L-methionine (SAM)-binding protein, essential for the L-[H-3-methyl]-methionine labelling of ORS571 Nod factors in vivo. Here, we present an in vitro assay showing that NodS from either A. caulinodans or Rhizobium species NGR234 methylates end-deacetylated chitooligosaccharides, using [H-3-methyl]-SAM as a methyl donor. The enzymatic and SAM-binding activity were correlated with the nodS gene and localized within the soluble protein fraction. The A. caulinodans nodS gene was expressed in Escherichia coil and a glutathione-S-transferase-NodS fusion protein purified. This protein bound SAM and could methylate end-deacetylated chitooligosaccharides, but could not fully methylate acetylated chitooligosaccharides or unmethylated lipo-chitooligosaccharides. These data implicate that the methylation step in the biosynthesis pathway of ORS571 Nod factors occurs after deacetylation and prior to acylation of the chitooligosaccharides.},
  author       = {Geelen, Danny and Leyman, Barbara and Mergaert, Peter and Klarskov, Klaus and Van Montagu, Marc and Geremia, Roberto and Holsters, Marcella},
  issn         = {0950-382X},
  journal      = {MOLECULAR MICROBIOLOGY},
  keyword      = {SESBANIA-ROSTRATA,NODULATION SIGNALS,STRAIN NGR234,BRADYRHIZOBIUM-JAPONICUM,AZORHIZOBIUM-CAULINODANS,LIPO-OLIGOSACCHARIDE SIGNALS,RHIZOBIUM-MELILOTI,HOST SPECIFICITY,GENES,IDENTIFICATION},
  language     = {eng},
  number       = {2},
  pages        = {387--397},
  title        = {NodS is a 5-adenosyl-L-methionine-dependent methyltransferase that methylates chitooligosaccharides deacetylated at the nonreducing end},
  url          = {http://dx.doi.org/10.1111/j.1365-2958.1995.mmi\_17020387.x},
  volume       = {17},
  year         = {1995},
}

Chicago
Geelen, Danny, Barbara Leyman, Peter Mergaert, Klaus Klarskov, Marc Van Montagu, Roberto Geremia, and Marcella Holsters. 1995. “NodS Is a 5-adenosyl-L-methionine-dependent Methyltransferase That Methylates Chitooligosaccharides Deacetylated at the Nonreducing End.” Molecular Microbiology 17 (2): 387–397.
APA
Geelen, D., Leyman, B., Mergaert, P., Klarskov, K., Van Montagu, M., Geremia, R., & Holsters, M. (1995). NodS is a 5-adenosyl-L-methionine-dependent methyltransferase that methylates chitooligosaccharides deacetylated at the nonreducing end. MOLECULAR MICROBIOLOGY, 17(2), 387–397.
Vancouver
1.
Geelen D, Leyman B, Mergaert P, Klarskov K, Van Montagu M, Geremia R, et al. NodS is a 5-adenosyl-L-methionine-dependent methyltransferase that methylates chitooligosaccharides deacetylated at the nonreducing end. MOLECULAR MICROBIOLOGY. 1995;17(2):387–97.
MLA
Geelen, Danny, Barbara Leyman, Peter Mergaert, et al. “NodS Is a 5-adenosyl-L-methionine-dependent Methyltransferase That Methylates Chitooligosaccharides Deacetylated at the Nonreducing End.” MOLECULAR MICROBIOLOGY 17.2 (1995): 387–397. Print.