Abstract
The Xenopus DG42 gene is expressed only between the late midblastula and neurulation stages of embryonic development. Recent database searches show that DG42 has striking sequence similarity to the Rhizobium NodC protein. NodC catalyzes the synthesis of chitin oligosaccharides which subsequently are transformed into bacterium-plant root signaling molecules. We find that the DG42 protein made in an in vitro coupled transcription-translation system catalyzes the synthesis of an array of chitin oligosaccharides. The result suggests the intriguing possibility that a bacterium-plant type of "Nod" signaling system may operate during early stages of vertebrate embryonic development and raises issues about the use of chitin synthase inhibitors as fungal-specific drugs.
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- Bulawa C. E., Wasco W. Chitin and nodulation. Nature. 1991 Oct 24;353(6346):710–710. doi: 10.1038/353710b0. [DOI] [PubMed] [Google Scholar]
- Cabib E. Differential inhibition of chitin synthetases 1 and 2 from Saccharomyces cerevisiae by polyoxin D and nikkomycins. Antimicrob Agents Chemother. 1991 Jan;35(1):170–173. doi: 10.1128/aac.35.1.170. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Jong A. J., Cordewener J., Lo Schiavo F., Terzi M., Vandekerckhove J., Van Kammen A., De Vries S. C. A carrot somatic embryo mutant is rescued by chitinase. Plant Cell. 1992 Apr;4(4):425–433. doi: 10.1105/tpc.4.4.425. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Jong A. J., Heidstra R., Spaink H. P., Hartog M. V., Meijer E. A., Hendriks T., Schiavo F. L., Terzi M., Bisseling T., Van Kammen A. Rhizobium Lipooligosaccharides Rescue a Carrot Somatic Embryo Mutant. Plant Cell. 1993 Jun;5(6):615–620. doi: 10.1105/tpc.5.6.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DeAngelis P. L., Yang N., Weigel P. H. The Streptococcus pyogenes hyaluronan synthase: sequence comparison and conservation among various group A strains. Biochem Biophys Res Commun. 1994 Feb 28;199(1):1–10. doi: 10.1006/bbrc.1994.1184. [DOI] [PubMed] [Google Scholar]
- Downie J. A. Signalling strategies for nodulation of legumes by rhizobia. Trends Microbiol. 1994 Sep;2(9):318–324. doi: 10.1016/0966-842x(94)90448-0. [DOI] [PubMed] [Google Scholar]
- Dénarié J., Cullimore J. Lipo-oligosaccharide nodulation factors: a minireview new class of signaling molecules mediating recognition and morphogenesis. Cell. 1993 Sep 24;74(6):951–954. doi: 10.1016/0092-8674(93)90717-5. [DOI] [PubMed] [Google Scholar]
- Ehrhardt D. W., Atkinson E. M., Long S. R. Depolarization of alfalfa root hair membrane potential by Rhizobium meliloti Nod factors. Science. 1992 May 15;256(5059):998–1000. doi: 10.1126/science.10744524. [DOI] [PubMed] [Google Scholar]
- Fisher R. F., Long S. R. Rhizobium--plant signal exchange. Nature. 1992 Jun 25;357(6380):655–660. doi: 10.1038/357655a0. [DOI] [PubMed] [Google Scholar]
- Geremia R. A., Mergaert P., Geelen D., Van Montagu M., Holsters M. The NodC protein of Azorhizobium caulinodans is an N-acetylglucosaminyltransferase. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2669–2673. doi: 10.1073/pnas.91.7.2669. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kang M. S., Elango N., Mattia E., Au-Young J., Robbins P. W., Cabib E. Isolation of chitin synthetase from Saccharomyces cerevisiae. Purification of an enzyme by entrapment in the reaction product. J Biol Chem. 1984 Dec 10;259(23):14966–14972. [PubMed] [Google Scholar]
- Nishimoto Y., Sakuda S., Takayama S., Yamada Y. Isolation and characterization of new allosamidins. J Antibiot (Tokyo) 1991 Jul;44(7):716–722. doi: 10.7164/antibiotics.44.716. [DOI] [PubMed] [Google Scholar]
- Robbins P. W., Albright C., Benfield B. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J Biol Chem. 1988 Jan 5;263(1):443–447. [PubMed] [Google Scholar]
- Robbins P. W., Overbye K., Albright C., Benfield B., Pero J. Cloning and high-level expression of chitinase-encoding gene of Streptomyces plicatus. Gene. 1992 Feb 1;111(1):69–76. doi: 10.1016/0378-1119(92)90604-n. [DOI] [PubMed] [Google Scholar]
- Roche P., Debellé F., Maillet F., Lerouge P., Faucher C., Truchet G., Dénarié J., Promé J. C. Molecular basis of symbiotic host specificity in Rhizobium meliloti: nodH and nodPQ genes encode the sulfation of lipo-oligosaccharide signals. Cell. 1991 Dec 20;67(6):1131–1143. doi: 10.1016/0092-8674(91)90290-f. [DOI] [PubMed] [Google Scholar]
- Rosa F., Sargent T. D., Rebbert M. L., Michaels G. S., Jamrich M., Grunz H., Jonas E., Winkles J. A., Dawid I. B. Accumulation and decay of DG42 gene products follow a gradient pattern during Xenopus embryogenesis. Dev Biol. 1988 Sep;129(1):114–123. doi: 10.1016/0012-1606(88)90166-2. [DOI] [PubMed] [Google Scholar]
- Sargent T. D., Dawid I. B. Differential gene expression in the gastrula of Xenopus laevis. Science. 1983 Oct 14;222(4620):135–139. doi: 10.1126/science.6688681. [DOI] [PubMed] [Google Scholar]
- Semino C. E., Dankert M. A. The in vitro biosynthesis of functional nodulation factors (Nod Rm) produced by Rhizobium meliloti 1021. Cell Mol Biol (Noisy-le-grand) 1994 Nov;40(7):1029–1037. [PubMed] [Google Scholar]
- Spaink H. P., Wijfjes A. H., van der Drift K. M., Haverkamp J., Thomas-Oates J. E., Lugtenberg B. J. Structural identification of metabolites produced by the NodB and NodC proteins of Rhizobium leguminosarum. Mol Microbiol. 1994 Sep;13(5):821–831. doi: 10.1111/j.1365-2958.1994.tb00474.x. [DOI] [PubMed] [Google Scholar]
- Vijn I., das Nevas L., van Kammen A., Franssen H., Bisseling T. Nod factors and nodulation in plants. Science. 1993 Jun 18;260(5115):1764–1765. doi: 10.1126/science.8511583. [DOI] [PubMed] [Google Scholar]