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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Sep 1;90(17):8005–8008. doi: 10.1073/pnas.90.17.8005

The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products.

D Kafetzopoulos 1, G Thireos 1, J N Vournakis 1, V Bouriotis 1
PMCID: PMC47276  PMID: 8367456

Abstract

Chitin deacetylase (EC 3.5.1.41) hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin. A cDNA to the Mucor rouxii mRNA encoding chitin deacetylase was isolated, characterized, and sequenced. Protein sequence comparisons revealed significant similarities of the fungal chitin deacetylase to rhizobial nodB proteins and to an uncharacterized protein encoded by a Bacillus stearothermophilus open reading frame. These data suggest the functional homology of these evolutionarily distant proteins. NodB is a chitooligosaccharide deacetylase essential for the biosynthesis of the bacterial nodulation signals, termed Nod factors. The observed similarity of chitin deacetylase to the B. stearothermophilus gene product suggests that this gene encodes a polysaccharide deacetylase.

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Selected References

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  1. Araki Y., Fukuoka S., Oba S., Ito E. Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls. Biochem Biophys Res Commun. 1971 Nov 5;45(3):751–758. doi: 10.1016/0006-291x(71)90481-5. [DOI] [PubMed] [Google Scholar]
  2. Araki Y., Ito E. A pathway of chitosan formation in Mucor rouxii. Enzymatic deacetylation of chitin. Eur J Biochem. 1975 Jun 16;55(1):71–78. doi: 10.1111/j.1432-1033.1975.tb02139.x. [DOI] [PubMed] [Google Scholar]
  3. Araki Y., Nakatani T., Nakayama K., Ito E. Occurrence of N-nonsubstituted glucosamine residues in peptidoglycan of lysozyme-resistant cell walls from Bacillus cereus. J Biol Chem. 1972 Oct 10;247(19):6312–6322. [PubMed] [Google Scholar]
  4. Atkinson E. M., Long S. R. Homology of Rhizobium meliloti NodC to polysaccharide polymerizing enzymes. Mol Plant Microbe Interact. 1992 Sep-Oct;5(5):439–442. doi: 10.1094/mpmi-5-439. [DOI] [PubMed] [Google Scholar]
  5. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. BARTNICKI-GARCIA S., NICKERSON W. J. Isolation, composition, and structure of cell walls of filamentous and yeast-like forms of Mucor rouxii. Biochim Biophys Acta. 1962 Mar 26;58:102–119. doi: 10.1016/0006-3002(62)90822-3. [DOI] [PubMed] [Google Scholar]
  7. Briza P., Ellinger A., Winkler G., Breitenbach M. Chemical composition of the yeast ascospore wall. The second outer layer consists of chitosan. J Biol Chem. 1988 Aug 15;263(23):11569–11574. [PubMed] [Google Scholar]
  8. Bulawa C. E. CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces cerevisiae: the CSD2 gene product is related to chitin synthases and to developmentally regulated proteins in Rhizobium species and Xenopus laevis. Mol Cell Biol. 1992 Apr;12(4):1764–1776. doi: 10.1128/mcb.12.4.1764. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  10. Church G. M., Gilbert W. Genomic sequencing. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1991–1995. doi: 10.1073/pnas.81.7.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Debellé F., Rosenberg C., Dénarié J. The Rhizobium, Bradyrhizobium, and Azorhizobium NodC proteins are homologous to yeast chitin synthases. Mol Plant Microbe Interact. 1992 Sep-Oct;5(5):443–446. doi: 10.1094/mpmi-5-443. [DOI] [PubMed] [Google Scholar]
  12. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Glisin V., Crkvenjakov R., Byus C. Ribonucleic acid isolated by cesium chloride centrifugation. Biochemistry. 1974 Jun 4;13(12):2633–2637. doi: 10.1021/bi00709a025. [DOI] [PubMed] [Google Scholar]
  14. Goethals K., Gao M., Tomekpe K., Van Montagu M., Holsters M. Common nodABC genes in Nod locus 1 of Azorhizobium caulinodans: nucleotide sequence and plant-inducible expression. Mol Gen Genet. 1989 Oct;219(1-2):289–298. doi: 10.1007/BF00261190. [DOI] [PubMed] [Google Scholar]
  15. John M., Röhrig H., Schmidt J., Wieneke U., Schell J. Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):625–629. doi: 10.1073/pnas.90.2.625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kafetzopoulos D., Martinou A., Bouriotis V. Bioconversion of chitin to chitosan: purification and characterization of chitin deacetylase from Mucor rouxii. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):2564–2568. doi: 10.1073/pnas.90.7.2564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Krishnan H. B., Pueppke S. G. Sequence and analysis of the nodABC region of Rhizobium fredii USDA257, a nitrogen-fixing symbiont of soybean and other legumes. Mol Plant Microbe Interact. 1991 Sep-Oct;4(5):512–520. doi: 10.1094/mpmi-4-512. [DOI] [PubMed] [Google Scholar]
  18. Lane W. S., Galat A., Harding M. W., Schreiber S. L. Complete amino acid sequence of the FK506 and rapamycin binding protein, FKBP, isolated from calf thymus. J Protein Chem. 1991 Apr;10(2):151–160. doi: 10.1007/BF01024778. [DOI] [PubMed] [Google Scholar]
  19. Lerouge P., Roche P., Faucher C., Maillet F., Truchet G., Promé J. C., Dénarié J. Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal. Nature. 1990 Apr 19;344(6268):781–784. doi: 10.1038/344781a0. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Schofield P. R., Watson J. M. DNA sequence of Rhizobium trifolii nodulation genes reveals a reiterated and potentially regulatory sequence preceding nodABC and nodFE. Nucleic Acids Res. 1986 Apr 11;14(7):2891–2903. doi: 10.1093/nar/14.7.2891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schultze M., Quiclet-Sire B., Kondorosi E., Virelizer H., Glushka J. N., Endre G., Géro S. D., Kondorosi A. Rhizobium meliloti produces a family of sulfated lipooligosaccharides exhibiting different degrees of plant host specificity. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):192–196. doi: 10.1073/pnas.89.1.192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Scott K. F. Conserved nodulation genes from the non-legume symbiont Bradyrhizobium sp. (Parasponia). Nucleic Acids Res. 1986 Apr 11;14(7):2905–2919. doi: 10.1093/nar/14.7.2905. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Short J. M., Fernandez J. M., Sorge J. A., Huse W. D. Lambda ZAP: a bacteriophage lambda expression vector with in vivo excision properties. Nucleic Acids Res. 1988 Aug 11;16(15):7583–7600. doi: 10.1093/nar/16.15.7583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Spaink H. P., Sheeley D. M., van Brussel A. A., Glushka J., York W. S., Tak T., Geiger O., Kennedy E. P., Reinhold V. N., Lugtenberg B. J. A novel highly unsaturated fatty acid moiety of lipo-oligosaccharide signals determines host specificity of Rhizobium. Nature. 1991 Nov 14;354(6349):125–130. doi: 10.1038/354125a0. [DOI] [PubMed] [Google Scholar]
  26. Török I., Kondorosi E., Stepkowski T., Pósfai J., Kondorosi A. Nucleotide sequence of Rhizobium meliloti nodulation genes. Nucleic Acids Res. 1984 Dec 21;12(24):9509–9524. doi: 10.1093/nar/12.24.9509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Török I., Kondorosi E., Stepkowski T., Pósfai J., Kondorosi A. Nucleotide sequence of Rhizobium meliloti nodulation genes. Nucleic Acids Res. 1984 Dec 21;12(24):9509–9524. doi: 10.1093/nar/12.24.9509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Vázquez M., Dávalos A., de las Peñas A., Sánchez F., Quinto C. Novel organization of the common nodulation genes in Rhizobium leguminosarum bv. phaseoli strains. J Bacteriol. 1991 Feb;173(3):1250–1258. doi: 10.1128/jb.173.3.1250-1258.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]

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