Molecular directionality of β-chitin biosynthesis

Journal of Molecular Biology

Volumn 286, Issue 1, 1999, Pages 247-255

  Sugiyama, Junji ^a   Boisset, Claire ^a   Hashimoto, Masayuki ^b   Watanabe, Takeshi ^b  

^a KYOTO UNIVERSITY   (Japan)

^b NIIGATA UNIVERSITY   (Japan)

Author keywords

Chain polarity; Chitinase A1; Microdiffraction; Reducing end; chitin

Indexed keywords

CHITIN; CHITINASE; POLYSACCHARIDE;

ARTICLE; BACILLUS CIRCULANS; CARBOHYDRATE SYNTHESIS; CRYSTALLOGRAPHY; DEGRADATION; DIATOM; DIFFRACTION; FIBER; MOLECULAR BIOLOGY; PRIORITY JOURNAL;

BACILLUS CIRCULANS; LAMELLIBRACHIA SATSUMA;

EID: 0033548191     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2458     Document Type: Article

References (35)

1. Albersheim P., Darvill A., Roberts K., Staehelin L. A., Varner J. E. Do the structure of cell wall polysaccharides define their mode of synthesis? Plant Physiol. 113:1997;1-3.
2. Armand S., Tomita H., Heyraud A., Gey C., Watanabe T., Henrissat B. Stereochemical course of the hydrolysis reaction catalysed by chitinases A1 and D from Bacillus circulans WL-12. FEBS Letters. 343:1994;177-180.
3. Atkins E. D. T. Conformations in polysaccharides and complex carbohydrates. Proc. Int. Symp. Biomol. Struct. Interact. Suppl. J. Biosci. 8:1985;375-387.
4. Barker C. E., Ruiz-Herrera J., Bartnicki-Garcia S. Structure and transformation of chitin synthetase particles (chitosomes) during microfibril synthesis in vitro. Proc. Natl Acad. Sci. USA. 73:1976;4570-4574.
5. Barr B. K., Hsieh Y.-L., Ganem B., Wilson D. B. Identification of two functionally different classes of exocellulases. Biochemistry. 35:1996;586-592.
6. Blackwell J. Structure of β-chitin or parallel chain systems of poly-β-(1-4)- N -acetyl- D -glucosamine. Biopolymers. 7:1969;281-298.
7. Blackwell J., Parker K. D., Rudall K. M. Chitin fibres of the diatoms Thalassiosira fluviatilis and Cyclotella cryptica. J. Mol. Biol. 28:1967;383-385.
8. Campbell J. A., Davies G. J., Bulone V., Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem. J. 326:1997;929-942.
9. Chanzy H. Chitin crystals. Domard A., Roberts G. A. F., Vårum K. M. Advances in Chitin Science. 1997;11-21 Jaques André Publications, Lyon.
10. French A., Howley P. S. Comparison of structures proposed for cellulose. Schuerch C. Cellulose and Wood - Chemistry and Technology. 1989;159-167 Wiley Interscience, New York.
11. Gaill F., Persson J., Sugiyama J., Vuong R., Chanzy H. The chitin system in the tubes of deep sea hydrothermal vent worms. J. Struct. Biol. 109:1992;116-128.
12. Gardner K. H., Blackwell J. Refinement of the structure of β-chitin. Biopolymers. 14:1975;1581-1595.
13. Hashimoto J., Miura T., Fujikura K., Ossaka J. Discovery of vestimentiferan tube-worms in the euphotic zone. Zool. Sci. 10:1993;1063-1067.
14. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:1991;309-316.
15. Herth W. The site of β-chitin fibril formation in centric diatoms. II. The chitin-forming cytoplasmic structures. J. Ultrastruct. Res. 68:1979;16-27.
16. Herth W., Barthlott W. The site of β-chitin fibril formation in centric diatoms. I. Pores and fibril formation. J. Ultrastruct. Res. 68:1979;6-15.
17. Kawagoe Y., Delmer D. P. Pathways and genes involved in cellulose biosynthesis. Genet. Eng. 19:1997;63-87.
18. Koyama M., Helbert W., Imai T., Sugiyama J., Henrissat B. Parallel-up structure evidences the molecular directionality during biosynthesis of bacterial cellulose. Proc. Natl Acad. Sci. USA. 94:1997;9091-9095.
19. Lindsay G. J. H., Gooday G. W. Action of chitinase on spines of the diatom Thalassiosira fluviatilis. Carbohydr. Res. 5:1985;131-140.
20. McLachlan J., McInnes A. G., Falk M. Studies on the chitan (chitin: poly- N -acetylglucosamine) fibers of the diatom Thalassiosira fluviatilis Hustedt. I. Production and isolation of chitan fibers. Canad. J. Bot. 43:1965;707-713.
21. Minke R., Blackwell J. The structure of α-chitin. J. Mol. Biol. 120:1978;167-181.
22. Nishitani K., Tominaga R. Endo-xyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule. J. Biol. Chem. 267:1992;21058-21064.
23. Rudall K. M. The chitin/protein complexes of insect cuticles. Advan. Insect Physiol. 1:1963;257-313.
24. Ruiz-Herrera J., Bartnicki-Garcia S. Synthesis of cell wall microfibrils in vitro by a "soluble" chitin synthetase from Mucor rouxii. Science. 186:1974;357-359.
25. Ruiz-Herrera J., Sing V. O., Van del Woude W. J., Bartinicki-Garcia S. Microfibril assembly by granules of chitin synthetase. Proc. Natl Acad. Sci. USA. 72:1975;2706-2710.
26. Ruiz-Herrera J., Bartnicki-Garcia S., Bracker C. E. Dissociation of chitosomes by digitonin into 16 S subunits with chitin synthetase activity. Biochim. Biophys. Acta. 629:1980;201-216.
27. Saito Y., Okano T., Chanzy H., Sugiyama J. Structural study of α-chitin from the grasping spines of the arrow worm (Sagitta spp.). J. Struct. Biol. 114:1995;218-228.
28. Saxena I. M., Brown R. M. Jr, Fevre M., Geremia R. A., Henrissat B. Multidomain architecture of β-glycosyl transferases: implications for mechanism of action. J. Bacteriol. 177:1995;1419-1424.
29. Schillito B., Lechaire J-P., Gaill F. Microvilli-like structures secreting chitin crytallites. J. Struct. Biol. 111:1993;59-67.
30. Semino C. E., Specht C. A., Raimondi A., Robbins P. W. Homologs of the Xenopus developmental gene DG42 are present in Zebrafish and mouse are involved in the synthesis of nod-like chitin oligosaccharides durin early embryogenesis. Proc. Natl Acad. Sci. USA. 93:1996;4548-4553.
31. Tadokoro H. Structure of Crystalline Polymers. 1979;Wiley, New York. p. 25-35.
32. Watanabe T., Oyanagi W., Suzuki K., Tanaka H. Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol. 172:1990a;4017-4022.
33. Watanabe T., Suzuki K., Oyanagi W., Ohnishi K., Tanaka H. Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship toSerratia chitinase and to the type III homology units of fibronectin. J. Biol. Chem. 265:1990b;15659-15665.
34. Watanabe T., Kobori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268:1993;18567-18572.
35. Watanabe T., Itoh Y., Yamada T., Hashimoto M., Sekine S., Tanaka H. The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 176:1994;4465-4472.