Skip to main content
NCBI home page
Genetics logoLink to Genetics
. 1998 Jun;149(2):843–856. doi: 10.1093/genetics/149.2.843

Involvement of protein N-glycosyl chain glucosylation and processing in the biosynthesis of cell wall beta-1,6-glucan of Saccharomyces cerevisiae.

S Shahinian 1, G J Dijkgraaf 1, A M Sdicu 1, D Y Thomas 1, C A Jakob 1, M Aebi 1, H Bussey 1
PMCID: PMC1460164  PMID: 9611196

Abstract

beta-1,6-Glucan plays a key structural role in the yeast cell wall. Of the genes involved in its biosynthesis, the activity of Cwh41p is known, i.e., the glucosidase I enzyme of protein N-chain glucose processing. We therefore examined the effects of N-chain glucosylation and processing mutants on beta-1,6-glucan biosynthesis and show that incomplete N-chain glucose processing results in a loss of beta-1,6-glucan, demonstrating a relationship between N-chain glucosylation/processing and beta-1,6-glucan biosynthesis. To explore the involvement of other N-chain-dependent events with beta-1,6-glucan synthesis, we investigated the Saccharomyces cerevisiae KRE5 and CNE1 genes, which encode homologs of the "quality control" components UDP-Glc:glycoprotein glucosyltransferase and calnexin, respectively. We show that the essential activity of Kre5p is separate from its possible role as a UDP-Glc:glycoprotein glucosyltransferase. We also observe a approximately 30% decrease in beta-1,6-glucan upon disruption of the CNE1 gene, a phenotype that is additive with other beta-1,6-glucan synthetic mutants. Analysis of the cell wall anchorage of the mannoprotein alpha-agglutinin suggests the existence of two beta-1,6-glucan biosynthetic pathways, one N-chain dependent, the other involving protein glycosylphosphatidylinositol modification.

Full Text

The Full Text of this article is available as a PDF (202.3 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Breuer W., Bause E. Oligosaccharyl transferase is a constitutive component of an oligomeric protein complex from pig liver endoplasmic reticulum. Eur J Biochem. 1995 Mar 15;228(3):689–696. [PubMed] [Google Scholar]
  2. Brown J. L., Bussey H. The yeast KRE9 gene encodes an O glycoprotein involved in cell surface beta-glucan assembly. Mol Cell Biol. 1993 Oct;13(10):6346–6356. doi: 10.1128/mcb.13.10.6346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brown J. L., Kossaczka Z., Jiang B., Bussey H. A mutational analysis of killer toxin resistance in Saccharomyces cerevisiae identifies new genes involved in cell wall (1-->6)-beta-glucan synthesis. Genetics. 1993 Apr;133(4):837–849. doi: 10.1093/genetics/133.4.837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Burda P., Aebi M. The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology. 1998 May;8(5):455–462. doi: 10.1093/glycob/8.5.455. [DOI] [PubMed] [Google Scholar]
  5. Burda P., te Heesen S., Brachat A., Wach A., Düsterhöft A., Aebi M. Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene encoding a putative mannosyl transferase. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7160–7165. doi: 10.1073/pnas.93.14.7160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bussey H. K1 killer toxin, a pore-forming protein from yeast. Mol Microbiol. 1991 Oct;5(10):2339–2343. doi: 10.1111/j.1365-2958.1991.tb02079.x. [DOI] [PubMed] [Google Scholar]
  7. Bussey H., Sacks W., Galley D., Saville D. Yeast killer plasmid mutations affecting toxin secretion and activity and toxin immunity function. Mol Cell Biol. 1982 Apr;2(4):346–354. doi: 10.1128/mcb.2.4.346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Caro L. H., Tettelin H., Vossen J. H., Ram A. F., van den Ende H., Klis F. M. In silicio identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae. Yeast. 1997 Dec;13(15):1477–1489. doi: 10.1002/(SICI)1097-0061(199712)13:15<1477::AID-YEA184>3.0.CO;2-L. [DOI] [PubMed] [Google Scholar]
  9. Chen D. C., Yang B. C., Kuo T. T. One-step transformation of yeast in stationary phase. Curr Genet. 1992 Jan;21(1):83–84. doi: 10.1007/BF00318659. [DOI] [PubMed] [Google Scholar]
  10. Chen M. H., Shen Z. M., Bobin S., Kahn P. C., Lipke P. N. Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a yeast cell wall protein with multiple immunoglobulin-like domains with atypical disulfides. J Biol Chem. 1995 Nov 3;270(44):26168–26177. doi: 10.1074/jbc.270.44.26168. [DOI] [PubMed] [Google Scholar]
  11. Choudhury P., Liu Y., Bick R. J., Sifers R. N. Intracellular association between UDP-glucose:glycoprotein glucosyltransferase and an incompletely folded variant of alpha1-antitrypsin. J Biol Chem. 1997 May 16;272(20):13446–13451. doi: 10.1074/jbc.272.20.13446. [DOI] [PubMed] [Google Scholar]
  12. Cid V. J., Durán A., del Rey F., Snyder M. P., Nombela C., Sánchez M. Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol Rev. 1995 Sep;59(3):345–386. doi: 10.1128/mr.59.3.345-386.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Dijkgraaf G. J., Brown J. L., Bussey H. The KNH1 gene of Saccharomyces cerevisiae is a functional homolog of KRE9. Yeast. 1996 Jun 15;12(7):683–692. doi: 10.1002/(SICI)1097-0061(19960615)12:7%3C683::AID-YEA959%3E3.0.CO;2-8. [DOI] [PubMed] [Google Scholar]
  14. Esmon B., Esmon P. C., Schekman R. Early steps in processing of yeast glycoproteins. J Biol Chem. 1984 Aug 25;259(16):10322–10327. [PubMed] [Google Scholar]
  15. Esmon P. C., Esmon B. E., Schauer I. E., Taylor A., Schekman R. Structure, assembly, and secretion of octameric invertase. J Biol Chem. 1987 Mar 25;262(9):4387–4394. [PubMed] [Google Scholar]
  16. Fernández F. S., Trombetta S. E., Hellman U., Parodi A. J. Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme fro Saccharomyces cerevisiae. J Biol Chem. 1994 Dec 2;269(48):30701–30706. [PubMed] [Google Scholar]
  17. Gietz R. D., Schiestl R. H., Willems A. R., Woods R. A. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast. 1995 Apr 15;11(4):355–360. doi: 10.1002/yea.320110408. [DOI] [PubMed] [Google Scholar]
  18. Hebert D. N., Foellmer B., Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell. 1995 May 5;81(3):425–433. doi: 10.1016/0092-8674(95)90395-x. [DOI] [PubMed] [Google Scholar]
  19. Heesen S., Lehle L., Weissmann A., Aebi M. Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae. Eur J Biochem. 1994 Aug 15;224(1):71–79. doi: 10.1111/j.1432-1033.1994.tb19996.x. [DOI] [PubMed] [Google Scholar]
  20. Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell. 1994 Mar;5(3):253–265. doi: 10.1091/mbc.5.3.253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Hill J. E., Myers A. M., Koerner T. J., Tzagoloff A. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast. 1986 Sep;2(3):163–167. doi: 10.1002/yea.320020304. [DOI] [PubMed] [Google Scholar]
  22. Hoffman C. S., Winston F. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene. 1987;57(2-3):267–272. doi: 10.1016/0378-1119(87)90131-4. [DOI] [PubMed] [Google Scholar]
  23. Huffaker T. C., Robbins P. W. Yeast mutants deficient in protein glycosylation. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7466–7470. doi: 10.1073/pnas.80.24.7466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Hutchins K., Bussey H. Cell wall receptor for yeast killer toxin: involvement of (1 leads to 6)-beta-D-glucan. J Bacteriol. 1983 Apr;154(1):161–169. doi: 10.1128/jb.154.1.161-169.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Jakob C. A., Burda P., te Heesen S., Aebi M., Roth J. Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo. Glycobiology. 1998 Feb;8(2):155–164. doi: 10.1093/glycob/8.2.155. [DOI] [PubMed] [Google Scholar]
  26. Jiang B., Sheraton J., Ram A. F., Dijkgraaf G. J., Klis F. M., Bussey H. CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in beta 1,6-glucan assembly. J Bacteriol. 1996 Feb;178(4):1162–1171. doi: 10.1128/jb.178.4.1162-1171.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Kapteyn J. C., Montijn R. C., Vink E., de la Cruz J., Llobell A., Douwes J. E., Shimoi H., Lipke P. N., Klis F. M. Retention of Saccharomyces cerevisiae cell wall proteins through a phosphodiester-linked beta-1,3-/beta-1,6-glucan heteropolymer. Glycobiology. 1996 Apr;6(3):337–345. doi: 10.1093/glycob/6.3.337. [DOI] [PubMed] [Google Scholar]
  28. Kilker R. D., Jr, Saunier B., Tkacz J. S., Herscovics A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J Biol Chem. 1981 May 25;256(10):5299–5603. [PubMed] [Google Scholar]
  29. Kollár R., Petráková E., Ashwell G., Robbins P. W., Cabib E. Architecture of the yeast cell wall. The linkage between chitin and beta(1-->3)-glucan. J Biol Chem. 1995 Jan 20;270(3):1170–1178. doi: 10.1074/jbc.270.3.1170. [DOI] [PubMed] [Google Scholar]
  30. Kollár R., Reinhold B. B., Petráková E., Yeh H. J., Ashwell G., Drgonová J., Kapteyn J. C., Klis F. M., Cabib E. Architecture of the yeast cell wall. Beta(1-->6)-glucan interconnects mannoprotein, beta(1-->)3-glucan, and chitin. J Biol Chem. 1997 Jul 11;272(28):17762–17775. doi: 10.1074/jbc.272.28.17762. [DOI] [PubMed] [Google Scholar]
  31. Kolodziej P. A., Young R. A. Epitope tagging and protein surveillance. Methods Enzymol. 1991;194:508–519. doi: 10.1016/0076-6879(91)94038-e. [DOI] [PubMed] [Google Scholar]
  32. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  33. Lu C. F., Kurjan J., Lipke P. N. A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin. Mol Cell Biol. 1994 Jul;14(7):4825–4833. doi: 10.1128/mcb.14.7.4825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Lu C. F., Montijn R. C., Brown J. L., Klis F., Kurjan J., Bussey H., Lipke P. N. Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall. J Cell Biol. 1995 Feb;128(3):333–340. doi: 10.1083/jcb.128.3.333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Lussier M., Sdicu A. M., Bussereau F., Jacquet M., Bussey H. The Ktr1p, Ktr3p, and Kre2p/Mnt1p mannosyltransferases participate in the elaboration of yeast O- and N-linked carbohydrate chains. J Biol Chem. 1997 Jun 13;272(24):15527–15531. doi: 10.1074/jbc.272.24.15527. [DOI] [PubMed] [Google Scholar]
  36. Lussier M., White A. M., Sheraton J., di Paolo T., Treadwell J., Southard S. B., Horenstein C. I., Chen-Weiner J., Ram A. F., Kapteyn J. C. Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics. 1997 Oct;147(2):435–450. doi: 10.1093/genetics/147.2.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Manners D. J., Masson A. J., Patterson J. C., Björndal H., Lindberg B. The structure of a beta-(1--6)-D-glucan from yeast cell walls. Biochem J. 1973 Sep;135(1):31–36. doi: 10.1042/bj1350031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Manners D. J., Masson A. J., Patterson J. C. The structure of a beta-(1 leads to 3)-D-glucan from yeast cell walls. Biochem J. 1973 Sep;135(1):19–30. doi: 10.1042/bj1350019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Meaden P., Hill K., Wagner J., Slipetz D., Sommer S. S., Bussey H. The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1----6)-beta-D-glucan synthesis and normal cell growth. Mol Cell Biol. 1990 Jun;10(6):3013–3019. doi: 10.1128/mcb.10.6.3013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Nakayama K., Nagasu T., Shimma Y., Kuromitsu J., Jigami Y. OCH1 encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine-linked oligosaccharides. EMBO J. 1992 Jul;11(7):2511–2519. doi: 10.1002/j.1460-2075.1992.tb05316.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Nuoffer C., Jenö P., Conzelmann A., Riezman H. Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane. Mol Cell Biol. 1991 Jan;11(1):27–37. doi: 10.1128/mcb.11.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Ora A., Helenius A. Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. J Biol Chem. 1995 Nov 3;270(44):26060–26062. doi: 10.1074/jbc.270.44.26060. [DOI] [PubMed] [Google Scholar]
  43. Ou W. J., Bergeron J. J., Li Y., Kang C. Y., Thomas D. Y. Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+. J Biol Chem. 1995 Jul 28;270(30):18051–18059. doi: 10.1074/jbc.270.30.18051. [DOI] [PubMed] [Google Scholar]
  44. Ou W. J., Cameron P. H., Thomas D. Y., Bergeron J. J. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature. 1993 Aug 26;364(6440):771–776. doi: 10.1038/364771a0. [DOI] [PubMed] [Google Scholar]
  45. Parlati F., Dominguez M., Bergeron J. J., Thomas D. Y. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem. 1995 Jan 6;270(1):244–253. doi: 10.1074/jbc.270.1.244. [DOI] [PubMed] [Google Scholar]
  46. Petrescu A. J., Butters T. D., Reinkensmeier G., Petrescu S., Platt F. M., Dwek R. A., Wormald M. R. The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 1997 Jul 16;16(14):4302–4310. doi: 10.1093/emboj/16.14.4302. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Ram A. F., Brekelmans S. S., Oehlen L. J., Klis F. M. Identification of two cell cycle regulated genes affecting the beta 1,3-glucan content of cell walls in Saccharomyces cerevisiae. FEBS Lett. 1995 Jan 23;358(2):165–170. doi: 10.1016/0014-5793(94)01418-z. [DOI] [PubMed] [Google Scholar]
  48. Ram A. F., Wolters A., Ten Hoopen R., Klis F. M. A new approach for isolating cell wall mutants in Saccharomyces cerevisiae by screening for hypersensitivity to calcofluor white. Yeast. 1994 Aug;10(8):1019–1030. doi: 10.1002/yea.320100804. [DOI] [PubMed] [Google Scholar]
  49. Raschke W. C., Kern K. A., Antalis C., Ballou C. E. Genetic control of yeast mannan structure. Isolation and characterization of mannan mutants. J Biol Chem. 1973 Jul 10;248(13):4660–4666. [PubMed] [Google Scholar]
  50. Reiss G., te Heesen S., Zimmerman J., Robbins P. W., Aebi M. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology. 1996 Jul;6(5):493–498. doi: 10.1093/glycob/6.5.493. [DOI] [PubMed] [Google Scholar]
  51. Roemer T., Bussey H. Yeast Kre1p is a cell surface O-glycoprotein. Mol Gen Genet. 1995 Nov 15;249(2):209–216. doi: 10.1007/BF00290368. [DOI] [PubMed] [Google Scholar]
  52. Roemer T., Paravicini G., Payton M. A., Bussey H. Characterization of the yeast (1-->6)-beta-glucan biosynthetic components, Kre6p and Skn1p, and genetic interactions between the PKC1 pathway and extracellular matrix assembly. J Cell Biol. 1994 Oct;127(2):567–579. doi: 10.1083/jcb.127.2.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Romero P. A., Dijkgraaf G. J., Shahinian S., Herscovics A., Bussey H. The yeast CWH41 gene encodes glucosidase I. Glycobiology. 1997 Oct;7(7):997–1004. doi: 10.1093/glycob/7.7.997. [DOI] [PubMed] [Google Scholar]
  54. Saunier B., Kilker R. D., Jr, Tkacz J. S., Quaroni A., Herscovics A. Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases. J Biol Chem. 1982 Dec 10;257(23):14155–14161. [PubMed] [Google Scholar]
  55. Schreuder M. P., Brekelmans S., van den Ende H., Klis F. M. Targeting of a heterologous protein to the cell wall of Saccharomyces cerevisiae. Yeast. 1993 Apr;9(4):399–409. doi: 10.1002/yea.320090410. [DOI] [PubMed] [Google Scholar]
  56. Sharma C. B., Lehle L., Tanner W. N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase. Eur J Biochem. 1981 May;116(1):101–108. doi: 10.1111/j.1432-1033.1981.tb05306.x. [DOI] [PubMed] [Google Scholar]
  57. Simons J. F., Ferro-Novick S., Rose M. D., Helenius A. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J Cell Biol. 1995 Jul;130(1):41–49. doi: 10.1083/jcb.130.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Sousa M. C., Ferrero-Garcia M. A., Parodi A. J. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry. 1992 Jan 14;31(1):97–105. doi: 10.1021/bi00116a015. [DOI] [PubMed] [Google Scholar]
  59. Stagljar I., te Heesen S., Aebi M. New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):5977–5981. doi: 10.1073/pnas.91.13.5977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Trombetta E. S., Simons J. F., Helenius A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem. 1996 Nov 1;271(44):27509–27516. doi: 10.1074/jbc.271.44.27509. [DOI] [PubMed] [Google Scholar]
  61. Trombetta S. E., Parodi A. J. Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem. 1992 May 5;267(13):9236–9240. [PubMed] [Google Scholar]
  62. Vai M., Gatti E., Lacanà E., Popolo L., Alberghina L. Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region. J Biol Chem. 1991 Jul 5;266(19):12242–12248. [PubMed] [Google Scholar]
  63. Vernet T., Dignard D., Thomas D. Y. A family of yeast expression vectors containing the phage f1 intergenic region. Gene. 1987;52(2-3):225–233. doi: 10.1016/0378-1119(87)90049-7. [DOI] [PubMed] [Google Scholar]
  64. Wach A., Brachat A., Pöhlmann R., Philippsen P. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast. 1994 Dec;10(13):1793–1808. doi: 10.1002/yea.320101310. [DOI] [PubMed] [Google Scholar]
  65. Wada I., Rindress D., Cameron P. H., Ou W. J., Doherty J. J., 2nd, Louvard D., Bell A. W., Dignard D., Thomas D. Y., Bergeron J. J. SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem. 1991 Oct 15;266(29):19599–19610. [PubMed] [Google Scholar]
  66. Yip C. L., Welch S. K., Klebl F., Gilbert T., Seidel P., Grant F. J., O'Hara P. J., MacKay V. L. Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2723–2727. doi: 10.1073/pnas.91.7.2723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. van Berkel M. A., Caro L. H., Montijn R. C., Klis F. M. Glucosylation of chimeric proteins in the cell wall of Saccharomyces cerevisiae. FEBS Lett. 1994 Jul 25;349(1):135–138. doi: 10.1016/0014-5793(94)00631-8. [DOI] [PubMed] [Google Scholar]

Articles from Genetics are provided here courtesy of Oxford University Press

RESOURCES