A Novel Family of Cell Wall-Related Proteins Regulated Differently during the Yeast Life Cycle

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Published inMolecular and Cellular Biology Vol. 20; no. 9; pp. 3245 - 3255
Main Authors Rodríguez-Peña, José Manuel, Cid, Víctor J., Arroyo, Javier, Nombela, César
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.05.2000
Taylor & Francis
Subjects
Online AccessGet full text
ISSN0270-7306
1098-5549
1067-8824
1098-5549
DOI10.1128/MCB.20.9.3245-3255.2000

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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial beta-glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamed CRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1Delta crh2Delta strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 and YLR213c (renamed CRR1, for CRH related) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial beta-glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamed CRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1Delta crh2Delta strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 and YLR213c (renamed CRR1, for CRH related) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial β-glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamedCRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1Δ crh2Δ strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 andYLR213c (renamed CRR1, for CRHrelated) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial beta -glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamed CRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1 Delta crh2 Delta strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 and YLR213c (renamed CRR1, for CRH related) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial β-glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamed CRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1Δ crh2Δ strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 and YLR213c (renamed CRR1, for CRH related) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1–green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial beta-glucanases and eukaryotic endotransglycosidases. Deletion of the corresponding genes, either individually or in combination, did not produce a lethal phenotype. However, the removal of YGR189c and YEL040w, but not YLR213c, caused additive sensitivity to compounds that interfere with cell wall construction, such as Congo red and Calcofluor White, and overexpression of YEL040w led to resistance to these compounds. These genes were renamed CRH1 and CRH2, respectively, for Congo red hypersensitive. By site-directed mutagenesis we found that the putative glycosidase domain of CRH1 was critical for its function in complementing hypersensitivity to the inhibitors. The involvement of CRH1 and CRH2 in the development of cell wall architecture was clearly shown, since the alkali-soluble glucan fraction in the crh1Delta crh2Delta strain was almost twice the level in the wild-type. Interestingly, the three genes were subject to different patterns of transcriptional regulation. CRH1 and YLR213c (renamed CRR1, for CRH related) were found to be cell cycle regulated and also expressed under sporulation conditions, whereas CRH2 expression did not vary during the mitotic cycle. Crh1 and Crh2 are localized at the cell surface, particularly in chitin-rich areas. Consistent with the observed expression patterns, Crh1-green fluorescent protein was found at the incipient bud site, around the septum area in later stages of budding, and in ascospore envelopes. Crh2 was found to localize mainly at the bud neck throughout the whole budding cycle, in mating projections and zygotes, but not in ascospores. These data suggest that the members of this family of putative glycosidases might exert a common role in cell wall organization at different stages of the yeast life cycle.
Author Javier Arroyo
José Manuel Rodríguez-Peña
César Nombela
Víctor J. Cid
AuthorAffiliation Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain
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  givenname: Víctor J.
  surname: Cid
  fullname: Cid, Víctor J.
  organization: Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain
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  organization: Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain
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  surname: Nombela
  fullname: Nombela, César
  organization: Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain
BackLink https://www.ncbi.nlm.nih.gov/pubmed/10757808$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1146/annurev.micro.52.1.687
10.1073/pnas.85.13.4735
10.1002/(SICI)1097-0061(19970330)13:4<357::AID-YEA77>3.0.CO;2-J
10.1093/genetics/147.2.435
10.1002/(SICI)1097-0061(19970915)13:11<1065::AID-YEA159>3.0.CO;2-K
10.1002/j.1460-2075.1996.tb00880.x
10.1007/s004380050706
10.1042/bj2820821
10.1046/j.1365-2958.1999.01320.x
10.1016/S0021-9258(19)74005-8
10.1074/jbc.270.3.1170
10.1002/yea.320100804
10.1083/jcb.114.1.111
10.1099/00221287-94-1-180
10.1083/jcb.143.6.1617
10.1021/bi980586q
10.1016/S0304-4165(98)00138-X
10.1111/j.1432-1033.1995.tb20399.x
10.1002/(SICI)1097-0061(199712)13:15<1477::AID-YEA184>3.0.CO;2-L
10.1046/j.1365-313X.1998.00239.x
10.1046/j.1365-2958.1999.01667.x
10.1007/BF00245214
10.1146/annurev.bi.51.070182.003555
10.1016/0092-8674(81)90059-3
10.1016/0076-6879(91)94055-H
10.1083/jcb.136.1.95
10.1074/jbc.272.28.17762
10.1128/jb.163.3.1180-1185.1985
10.1002/(SICI)1097-0061(199707)13:9<837::AID-YEA145>3.0.CO;2-T
10.1128/JB.180.15.3735-3740.1998
10.1002/(SICI)1097-0061(19980630)14:9<853::AID-YEA274>3.0.CO;2-O
10.1006/jmbi.1993.1518
10.1016/0378-1119(88)90185-0
10.1128/aem.60.4.1213-1220.1994
10.1002/yea.320101208
10.1016/S0021-9258(17)36655-3
10.1083/jcb.139.1.75
10.1042/bj3160695
10.1083/jcb.127.2.567
10.1002/yea.320020304
10.1016/S0304-4165(98)00137-8
10.1128/jb.171.11.6259-6264.1989
10.1128/jb.175.7.2102-2106.1993
10.1128/jb.179.7.2154-2162.1997
10.1093/genetics/122.1.19
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Corresponding author. Mailing address: Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, 28040 Madrid, Spain. Phone: 34 91 3941746. Fax: 34 91 3941745. E-mail: jarroyo@eucmax.sim.ucm.es.
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References Sikorski R. S. (B46) 1989; 122
Kopecka M. (B28) 1992; 158
Tabernero C. (B48) 1994; 60
Silverman S. J. (B47) 1988; 85
DeMarini D. J. (B6) 1997; 139
Santos B. (B44) 1997; 136
Mrsa V. (B35) 1993; 175
Campbell P. (B4) 1998; 15
Goldman R. C. (B13) 1995; 227
McKnight G. L. (B32) 1981; 25
Fry S. C. (B9) 1992; 282
Jimenez J. (B20) 1998; 143
Viladot J. L. (B49) 1998; 37
Moukadiri I. (B34) 1997; 179
Pringle J. R. (B38) 1991; 194
Fleet G. H. (B8) 1976; 94
Igual J. C. (B19) 1996; 15
Caro L. H. P. (B5) 1997; 13
Popolo L. (B37) 1999; 1426
Arroyo J. (B1) 1997; 13
Gietz R. D. (B11) 1988; 74
Kapteyn J. C. (B24) 1999; 31
Wach A. (B50) 1997; 13
Ausubel F. M. (B2) 1993
Rodriguez-Peña J. M. (B40) 1998; 14
Ram A. F. J. (B39) 1994; 10
Hoj P. B. (B18) 1992; 267
Roemer T. (B41) 1994; 127
Hill J. E. (B17) 1986; 2
Gari E. (B10) 1997; 13
Jung U. S. (B22) 1999; 34
Gietz R. D. (B12) 1994
Kapteyn J. C. (B23) 1999; 1426
Orlean P. (B36) 1997
Kollár R. (B27) 1997; 272
Juncosa M. (B21) 1994; 269
Melnick L. (B33) 1993; 233
Shaw J. A. (B45) 1991; 114
Cabib E. (B3) 1982; 51
Kollár R. (B26) 1995; 270
Madden K. (B31) 1998; 52
Hartland R. P. (B15) 1994; 10
Henrissat B. (B16) 1996; 316
Fleet G. H. (B7) 1991
Roncero C. (B42) 1985; 163
Hamada K. (B14) 1998; 258
Lussier M. (B30) 1997; 147
Sambrook J. (B43) 1989
Klebl F. (B25) 1989; 171
Lipke P. N. (B29) 1998; 180
References_xml – volume: 52
  start-page: 687
  year: 1998
  ident: B31
  publication-title: Annu. Rev. Microbiol.
  doi: 10.1146/annurev.micro.52.1.687
– volume: 85
  start-page: 4735
  year: 1988
  ident: B47
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.85.13.4735
– volume: 13
  start-page: 357
  year: 1997
  ident: B1
  publication-title: Yeast
  doi: 10.1002/(SICI)1097-0061(19970330)13:4<357::AID-YEA77>3.0.CO;2-J
– volume: 147
  start-page: 435
  year: 1997
  ident: B30
  publication-title: Genetics
  doi: 10.1093/genetics/147.2.435
– volume: 13
  start-page: 1065
  year: 1997
  ident: B50
  publication-title: Yeast
  doi: 10.1002/(SICI)1097-0061(19970915)13:11<1065::AID-YEA159>3.0.CO;2-K
– volume: 15
  start-page: 5001
  year: 1996
  ident: B19
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1996.tb00880.x
– volume: 258
  start-page: 53
  year: 1998
  ident: B14
  publication-title: Mol. Gen. Genet.
  doi: 10.1007/s004380050706
– volume: 282
  start-page: 821
  year: 1992
  ident: B9
  publication-title: Biochem. J.
  doi: 10.1042/bj2820821
– volume: 31
  start-page: 1835
  year: 1999
  ident: B24
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.1999.01320.x
– volume: 267
  start-page: 25059
  year: 1992
  ident: B18
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)74005-8
– volume: 270
  start-page: 1170
  year: 1995
  ident: B26
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.270.3.1170
– volume: 10
  start-page: 1019
  year: 1994
  ident: B39
  publication-title: Yeast
  doi: 10.1002/yea.320100804
– volume: 114
  start-page: 111
  year: 1991
  ident: B45
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.114.1.111
– volume: 94
  start-page: 180
  year: 1976
  ident: B8
  publication-title: J. Gen. Microbiol.
  doi: 10.1099/00221287-94-1-180
– start-page: 199
  volume-title: The yeasts.
  year: 1991
  ident: B7
– volume: 143
  start-page: 1617
  year: 1998
  ident: B20
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.143.6.1617
– volume: 37
  start-page: 11332
  year: 1998
  ident: B49
  publication-title: Biochemistry
  doi: 10.1021/bi980586q
– volume: 1426
  start-page: 385
  year: 1999
  ident: B37
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/S0304-4165(98)00138-X
– volume: 227
  start-page: 372
  year: 1995
  ident: B13
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1995.tb20399.x
– volume: 13
  start-page: 1477
  year: 1997
  ident: B5
  publication-title: Yeast
  doi: 10.1002/(SICI)1097-0061(199712)13:15<1477::AID-YEA184>3.0.CO;2-L
– volume: 15
  start-page: 553
  year: 1998
  ident: B4
  publication-title: Plant J.
  doi: 10.1046/j.1365-313X.1998.00239.x
– volume: 34
  start-page: 1049
  year: 1999
  ident: B22
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.1999.01667.x
– volume: 158
  start-page: 115
  year: 1992
  ident: B28
  publication-title: Arch. Microbiol.
  doi: 10.1007/BF00245214
– start-page: 121
  volume-title: Molecular genetics of yeast: a practical approach.
  year: 1994
  ident: B12
– volume: 51
  start-page: 763
  year: 1982
  ident: B3
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.bi.51.070182.003555
– volume: 25
  start-page: 409
  year: 1981
  ident: B32
  publication-title: Cell
  doi: 10.1016/0092-8674(81)90059-3
– start-page: 229
  volume-title: Molecular and cellular biology of the yeast Saccharomyces.
  year: 1997
  ident: B36
– volume: 194
  start-page: 732
  year: 1991
  ident: B38
  publication-title: Methods Enzymol.
  doi: 10.1016/0076-6879(91)94055-H
– volume: 136
  start-page: 95
  year: 1997
  ident: B44
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.136.1.95
– volume: 272
  start-page: 17762
  year: 1997
  ident: B27
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.28.17762
– volume: 163
  start-page: 1180
  year: 1985
  ident: B42
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.163.3.1180-1185.1985
– volume-title: Molecular cloning: a laboratory manual.
  year: 1989
  ident: B43
– volume-title: Current protocols in molecular biology.
  year: 1993
  ident: B2
– volume: 13
  start-page: 837
  year: 1997
  ident: B10
  publication-title: Yeast
  doi: 10.1002/(SICI)1097-0061(199707)13:9<837::AID-YEA145>3.0.CO;2-T
– volume: 180
  start-page: 3735
  year: 1998
  ident: B29
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.180.15.3735-3740.1998
– volume: 14
  start-page: 853
  year: 1998
  ident: B40
  publication-title: Yeast
  doi: 10.1002/(SICI)1097-0061(19980630)14:9<853::AID-YEA274>3.0.CO;2-O
– volume: 233
  start-page: 372
  year: 1993
  ident: B33
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1993.1518
– volume: 74
  start-page: 527
  year: 1988
  ident: B11
  publication-title: Gene
  doi: 10.1016/0378-1119(88)90185-0
– volume: 60
  start-page: 1213
  year: 1994
  ident: B48
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/aem.60.4.1213-1220.1994
– volume: 10
  start-page: 1591
  year: 1994
  ident: B15
  publication-title: Yeast
  doi: 10.1002/yea.320101208
– volume: 269
  start-page: 14530
  year: 1994
  ident: B21
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)36655-3
– volume: 139
  start-page: 75
  year: 1997
  ident: B6
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.139.1.75
– volume: 316
  start-page: 695
  year: 1996
  ident: B16
  publication-title: Biochem. J.
  doi: 10.1042/bj3160695
– volume: 127
  start-page: 567
  year: 1994
  ident: B41
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.127.2.567
– volume: 2
  start-page: 163
  year: 1986
  ident: B17
  publication-title: Yeast
  doi: 10.1002/yea.320020304
– volume: 1426
  start-page: 373
  year: 1999
  ident: B23
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/S0304-4165(98)00137-8
– volume: 171
  start-page: 6259
  year: 1989
  ident: B25
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.171.11.6259-6264.1989
– volume: 175
  start-page: 2102
  year: 1993
  ident: B35
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.175.7.2102-2106.1993
– volume: 179
  start-page: 2154
  year: 1997
  ident: B34
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.179.7.2154-2162.1997
– volume: 122
  start-page: 19
  year: 1989
  ident: B46
  publication-title: Genetics
  doi: 10.1093/genetics/122.1.19
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial β-glucanases...
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial...
The Saccharomyces cerevisiae Ygr189c, Yel040w, and Ylr213c gene products show significant homologies among themselves and with various bacterial beta...
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SubjectTerms Alleles
Amino Acid Sequence
Benzenesulfonates - pharmacology
Cell Growth and Development
Cell Wall - metabolism
Cell Wall - physiology
Congo Red - pharmacology
CRH1 gene
CRH2 gene
Gene Expression Regulation, Fungal
Glucans - metabolism
Glycoside Hydrolases - genetics
Glycoside Hydrolases - metabolism
Glycoside Hydrolases - physiology
Green Fluorescent Proteins
Luminescent Proteins - metabolism
Microscopy, Confocal
Molecular Sequence Data
Multigene Family
Mutagenesis, Site-Directed
Open Reading Frames
Phenotype
Recombinant Fusion Proteins - metabolism
RNA, Messenger - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
Time Factors
Transcription, Genetic
Yel040w protein
Ygr189c protein
Ylr213c protein
Title A Novel Family of Cell Wall-Related Proteins Regulated Differently during the Yeast Life Cycle
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