Found 3 records.
Displayed records from 1 to 3
Expand all records
Collapse all records
Show all as text (SweetDB notation)
Show all graphically (SNFG notation)
Felle HH, Kondorosi E, Kondorosi A, Schultze M
Nod signal-induced plasma membrane potential changes in alfalfa root hairs are differentially sensitive to structural modifications of the lipochitooligosaccharide
Plant Journal: for Cell and Molecular Biology 7 (1995)
939-947
S-6)-+
|
Pam-(1-2)-b-D-GlcpN-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Rhizobium meliloti
(later renamed to: Sinorhizobium meliloti)
(NCBI TaxID 382,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Publication DOI: 10.1046/j.1365-313X.1995.07060939.xJournal NLM ID: 9207397Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
Institutions: Institut des Sciences Végétales, CNRS, Gif-sur-Yvette, France, Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary, Botanisches Institut I, Universität Giessen, Giessen, Germany
Lipochitooligosaccharide Nod signals are important determinants of host specificity in the Rhizobium-legume symbiosis. The most rapid response of plant cells to the R. meliloti Nod signal NodRm-IV(C16:2,S) reported so far is the depolarization of the plasma membrane potential in alfalfa root hairs. In order to investigate whether this response may be part of a specific signal transduction cascade involved in the nodulation process, its specificity was studied with respect to host-specific modifications of the lipochitooligosaccharide. Five different Nod factors displaying different degrees of activity in inducing root hair deformation or cortical cell divisions on alfalfa were tested. The ability of the Nod factors to elicit plasma membrane depolarization correlated well with their activity in the bioassays. Removal of the sulfate group (NodRm-IV(C16:2)) led to inactivation of the Nod factor. An increase in the length of the chitooligosaccharide backbone (NodRm-V(C16:2,S)) or saturation of the acyl chain (NodRm-IV(C16:0,S)) resulted in severely reduced activity. In contrast, the O-acetyl group at the non-reducing terminus in NodRm-IV(Ac,C16:2,S), which confers substantially higher activity in long-term bioassays, did not enhance plasma membrane depolarization significantly in comparison with the non-O-acetylated factor. Thus, the rapid plasma membrane response is differentially sensitive to various structural motifs of the lipochitooligosaccharide. These data suggest that the different substituents modifying the basic Nod factor structure may have distinct functions, not all of them contributing to the interaction with a putative receptor in root hair cells. However, the overall specificity of the membrane depolarization for the cognate Nod factors raises the possibility that it is involved in a Nod signal transduction pathway.
Structure type: oligomer
Trivial name: NodRm-IV(C16:0,S)
Compound class: LOS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141181,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_153212,IEDB_1635956,IEDB_241099,IEDB_241119,IEDB_241120,SB_74,SB_85
Methods: plant assays, plasma membrane potential, conductance measurment
Biological activity: Nod factor
NCBI Taxonomy refs (TaxIDs): 382Reference(s) to other database(s): CCSD:
50002, CBank-STR:10155
Show glycosyltransferases
There is only one chemically distinct structure:
Expand this record
Collapse this record
Felle HH, Kondorosi E, Kondorosi A, Schultze M
Nod signal-induced plasma membrane potential changes in alfalfa root hairs are differentially sensitive to structural modifications of the lipochitooligosaccharide
Plant Journal: for Cell and Molecular Biology 7 (1995)
939-947
S-6)-+
|
C16={?,?}-(1-2)-b-D-GlcpN-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Rhizobium meliloti
(later renamed to: Sinorhizobium meliloti)
(NCBI TaxID 382,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Publication DOI: 10.1046/j.1365-313X.1995.07060939.xJournal NLM ID: 9207397Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
Institutions: Institut des Sciences Végétales, CNRS, Gif-sur-Yvette, France, Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary, Botanisches Institut I, Universität Giessen, Giessen, Germany
Lipochitooligosaccharide Nod signals are important determinants of host specificity in the Rhizobium-legume symbiosis. The most rapid response of plant cells to the R. meliloti Nod signal NodRm-IV(C16:2,S) reported so far is the depolarization of the plasma membrane potential in alfalfa root hairs. In order to investigate whether this response may be part of a specific signal transduction cascade involved in the nodulation process, its specificity was studied with respect to host-specific modifications of the lipochitooligosaccharide. Five different Nod factors displaying different degrees of activity in inducing root hair deformation or cortical cell divisions on alfalfa were tested. The ability of the Nod factors to elicit plasma membrane depolarization correlated well with their activity in the bioassays. Removal of the sulfate group (NodRm-IV(C16:2)) led to inactivation of the Nod factor. An increase in the length of the chitooligosaccharide backbone (NodRm-V(C16:2,S)) or saturation of the acyl chain (NodRm-IV(C16:0,S)) resulted in severely reduced activity. In contrast, the O-acetyl group at the non-reducing terminus in NodRm-IV(Ac,C16:2,S), which confers substantially higher activity in long-term bioassays, did not enhance plasma membrane depolarization significantly in comparison with the non-O-acetylated factor. Thus, the rapid plasma membrane response is differentially sensitive to various structural motifs of the lipochitooligosaccharide. These data suggest that the different substituents modifying the basic Nod factor structure may have distinct functions, not all of them contributing to the interaction with a putative receptor in root hair cells. However, the overall specificity of the membrane depolarization for the cognate Nod factors raises the possibility that it is involved in a Nod signal transduction pathway.
Structure type: oligomer
Trivial name: NodRm-IV(C16:2,S), NodRm-V(C16:2,S)
Compound class: LOS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_153212,IEDB_1635956,IEDB_241099,IEDB_241119,IEDB_241120,SB_74,SB_85
Methods: plant assays, plasma membrane potential, conductance measurment
Biological activity: Nod factor
NCBI Taxonomy refs (TaxIDs): 382Reference(s) to other database(s): CCSD:
50001, CBank-STR:10158
Show glycosyltransferases
There is only one chemically distinct structure:
Expand this record
Collapse this record
Felle HH, Kondorosi E, Kondorosi A, Schultze M
Nod signal-induced plasma membrane potential changes in alfalfa root hairs are differentially sensitive to structural modifications of the lipochitooligosaccharide
Plant Journal: for Cell and Molecular Biology 7 (1995)
939-947
S-6)-+
|
C16={?,?}-(1-2)-b-D-GlcpN6Ac-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
Show graphically |
Rhizobium meliloti
(later renamed to: Sinorhizobium meliloti)
(NCBI TaxID 382,
species name lookup)
Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Publication DOI: 10.1046/j.1365-313X.1995.07060939.xJournal NLM ID: 9207397Publisher: Oxford: Blackwell Scientific Publishers and BIOS Scientific Publishers for the Society for Experimental Biology
Institutions: Institut des Sciences Végétales, CNRS, Gif-sur-Yvette, France, Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary, Botanisches Institut I, Universität Giessen, Giessen, Germany
Lipochitooligosaccharide Nod signals are important determinants of host specificity in the Rhizobium-legume symbiosis. The most rapid response of plant cells to the R. meliloti Nod signal NodRm-IV(C16:2,S) reported so far is the depolarization of the plasma membrane potential in alfalfa root hairs. In order to investigate whether this response may be part of a specific signal transduction cascade involved in the nodulation process, its specificity was studied with respect to host-specific modifications of the lipochitooligosaccharide. Five different Nod factors displaying different degrees of activity in inducing root hair deformation or cortical cell divisions on alfalfa were tested. The ability of the Nod factors to elicit plasma membrane depolarization correlated well with their activity in the bioassays. Removal of the sulfate group (NodRm-IV(C16:2)) led to inactivation of the Nod factor. An increase in the length of the chitooligosaccharide backbone (NodRm-V(C16:2,S)) or saturation of the acyl chain (NodRm-IV(C16:0,S)) resulted in severely reduced activity. In contrast, the O-acetyl group at the non-reducing terminus in NodRm-IV(Ac,C16:2,S), which confers substantially higher activity in long-term bioassays, did not enhance plasma membrane depolarization significantly in comparison with the non-O-acetylated factor. Thus, the rapid plasma membrane response is differentially sensitive to various structural motifs of the lipochitooligosaccharide. These data suggest that the different substituents modifying the basic Nod factor structure may have distinct functions, not all of them contributing to the interaction with a putative receptor in root hair cells. However, the overall specificity of the membrane depolarization for the cognate Nod factors raises the possibility that it is involved in a Nod signal transduction pathway.
Structure type: oligomer
Trivial name: NodRm-IV(Ac,C16:2,S)
Compound class: LOS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_153212,IEDB_1635956,IEDB_241099,IEDB_241119,IEDB_241120,SB_74,SB_85
Methods: plant assays, plasma membrane potential, conductance measurment
Biological activity: Nod factor
NCBI Taxonomy refs (TaxIDs): 382Reference(s) to other database(s): CCSD:
50003, CBank-STR:13186
Show glycosyltransferases
There is only one chemically distinct structure:
Expand this record
Collapse this record
Total list of record IDs on all result pages of the current query:
Execution: 8 sec