Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation
This paper reports a phenotypic characterization of ggp1 mutants. The cloned GGP1 (GAS1) gene, which encodes a major GPI-anchored glycoprotein (gp115) of Saccharomyces cerevisiae of unknown function, was used to direct the inactivation of the chromosomal gene in haploid and diploid strains by gene r...
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| Veröffentlicht in: | Journal of Bacteriology 1993-04, Vol.175 (7), p.1879-1885 |
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| creator | Popolo, L. (Universita degli Studi di Milano, Milan, Italy) Vai, M Gatti, E Porello, S Bonfante, P Balestrini, R Alberghina, L |
| description | This paper reports a phenotypic characterization of ggp1 mutants. The cloned GGP1 (GAS1) gene, which encodes a major GPI-anchored glycoprotein (gp115) of Saccharomyces cerevisiae of unknown function, was used to direct the inactivation of the chromosomal gene in haploid and diploid strains by gene replacement. The analysis of the null mutants reveals a reduction in the growth rate of 15 to 40%. Cells are round, with more than one bud, and extensively vacuolized. In the stationary phase, mutant cells are very large, arrest with a high percentage of budded cells (about 54 and 70% for haploid and diploid null mutants, respectively, in comparison with about 10 to 13% for control cells), and have reduced viability. The observed phenotype suggests defects in cell separation. Flow cytometric analysis of DNA reveals an increase in the fraction of cells in the G2+M+G1 compartment during exponential growth. Conjugation and sporulation are not affected. The exocellular location of gp115 led us to examine cell wall properties. Cell wall and septum ultrastructure of abnormally budded cells was analyzed by electron microscopy analysis, and no appreciable differences from wild-type cells were found. Microscopic analysis revealed an increase in chitin content and delocalization. In comparison with control cells, ggp1 null mutants are shown to be resistant to Zymolyase during the exponential growth phase. A fivefold overexpression of gp115 does not bring about any effects on cell growth parameters and cell wall properties |
| doi_str_mv | 10.1128/jb.175.7.1879-1885.1993 |
| format | Article |
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(Universita degli Studi di Milano, Milan, Italy) ; Vai, M ; Gatti, E ; Porello, S ; Bonfante, P ; Balestrini, R ; Alberghina, L</creator><creatorcontrib>Popolo, L. (Universita degli Studi di Milano, Milan, Italy) ; Vai, M ; Gatti, E ; Porello, S ; Bonfante, P ; Balestrini, R ; Alberghina, L</creatorcontrib><description>This paper reports a phenotypic characterization of ggp1 mutants. The cloned GGP1 (GAS1) gene, which encodes a major GPI-anchored glycoprotein (gp115) of Saccharomyces cerevisiae of unknown function, was used to direct the inactivation of the chromosomal gene in haploid and diploid strains by gene replacement. The analysis of the null mutants reveals a reduction in the growth rate of 15 to 40%. Cells are round, with more than one bud, and extensively vacuolized. In the stationary phase, mutant cells are very large, arrest with a high percentage of budded cells (about 54 and 70% for haploid and diploid null mutants, respectively, in comparison with about 10 to 13% for control cells), and have reduced viability. The observed phenotype suggests defects in cell separation. Flow cytometric analysis of DNA reveals an increase in the fraction of cells in the G2+M+G1 compartment during exponential growth. Conjugation and sporulation are not affected. The exocellular location of gp115 led us to examine cell wall properties. Cell wall and septum ultrastructure of abnormally budded cells was analyzed by electron microscopy analysis, and no appreciable differences from wild-type cells were found. Microscopic analysis revealed an increase in chitin content and delocalization. In comparison with control cells, ggp1 null mutants are shown to be resistant to Zymolyase during the exponential growth phase. A fivefold overexpression of gp115 does not bring about any effects on cell growth parameters and cell wall properties</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>EISSN: 1067-8832</identifier><identifier>DOI: 10.1128/jb.175.7.1879-1885.1993</identifier><identifier>PMID: 8458831</identifier><identifier>CODEN: JOBAAY</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Bacteriology ; BIOCHIMIE ; Biological and medical sciences ; BIOQUIMICA ; Cell Division - physiology ; Cell Wall - chemistry ; Cellular biology ; CHITINE ; Conjugation, Genetic ; DIFERENCIACION CELULAR ; DIFFERENCIATION CELLULAIRE ; Diploidy ; DIVISION CELLULAIRE ; DIVISION CELULAR ; ESTRUCTURA CELULAR ; Fundamental and applied biological sciences. Psychology ; G1 Phase ; G2 Phase ; GENE ; GENES ; Genes, Fungal - genetics ; GLICOLIPIDOS ; GLICOPROTEINAS ; Glucan Endo-1,3-beta-D-Glucosidase - pharmacology ; GLYCOLIPIDE ; GLYCOPROTEINE ; Haploidy ; INOSITOL ; Membrane Glycoproteins - genetics ; Microbiology ; Mitosis ; Morphogenesis - physiology ; Morphology, structure, chemical composition ; Mutagenesis, Insertional ; MUTANT ; MUTANTES ; Mutation ; Mycology ; PARED CELULAR ; PAROI CELLULAIRE ; Phenotype ; Proteins ; QUITINA ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - physiology ; Saccharomyces cerevisiae - ultrastructure ; Saccharomyces cerevisiae Proteins ; Spores, Fungal - growth & development ; STRUCTURE CELLULAIRE</subject><ispartof>Journal of Bacteriology, 1993-04, Vol.175 (7), p.1879-1885</ispartof><rights>1993 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Apr 1993</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c663t-3a9c7e8250b9992dc06378399080e37d727cdd19955d805acd9be7280ff60b213</citedby><cites>FETCH-LOGICAL-c663t-3a9c7e8250b9992dc06378399080e37d727cdd19955d805acd9be7280ff60b213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC204249/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC204249/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4709391$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8458831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Popolo, L. (Universita degli Studi di Milano, Milan, Italy)</creatorcontrib><creatorcontrib>Vai, M</creatorcontrib><creatorcontrib>Gatti, E</creatorcontrib><creatorcontrib>Porello, S</creatorcontrib><creatorcontrib>Bonfante, P</creatorcontrib><creatorcontrib>Balestrini, R</creatorcontrib><creatorcontrib>Alberghina, L</creatorcontrib><title>Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation</title><title>Journal of Bacteriology</title><addtitle>J Bacteriol</addtitle><description>This paper reports a phenotypic characterization of ggp1 mutants. The cloned GGP1 (GAS1) gene, which encodes a major GPI-anchored glycoprotein (gp115) of Saccharomyces cerevisiae of unknown function, was used to direct the inactivation of the chromosomal gene in haploid and diploid strains by gene replacement. The analysis of the null mutants reveals a reduction in the growth rate of 15 to 40%. Cells are round, with more than one bud, and extensively vacuolized. In the stationary phase, mutant cells are very large, arrest with a high percentage of budded cells (about 54 and 70% for haploid and diploid null mutants, respectively, in comparison with about 10 to 13% for control cells), and have reduced viability. The observed phenotype suggests defects in cell separation. Flow cytometric analysis of DNA reveals an increase in the fraction of cells in the G2+M+G1 compartment during exponential growth. Conjugation and sporulation are not affected. The exocellular location of gp115 led us to examine cell wall properties. Cell wall and septum ultrastructure of abnormally budded cells was analyzed by electron microscopy analysis, and no appreciable differences from wild-type cells were found. Microscopic analysis revealed an increase in chitin content and delocalization. In comparison with control cells, ggp1 null mutants are shown to be resistant to Zymolyase during the exponential growth phase. A fivefold overexpression of gp115 does not bring about any effects on cell growth parameters and cell wall properties</description><subject>Bacteriology</subject><subject>BIOCHIMIE</subject><subject>Biological and medical sciences</subject><subject>BIOQUIMICA</subject><subject>Cell Division - physiology</subject><subject>Cell Wall - chemistry</subject><subject>Cellular biology</subject><subject>CHITINE</subject><subject>Conjugation, Genetic</subject><subject>DIFERENCIACION CELULAR</subject><subject>DIFFERENCIATION CELLULAIRE</subject><subject>Diploidy</subject><subject>DIVISION CELLULAIRE</subject><subject>DIVISION CELULAR</subject><subject>ESTRUCTURA CELULAR</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>G1 Phase</subject><subject>G2 Phase</subject><subject>GENE</subject><subject>GENES</subject><subject>Genes, Fungal - genetics</subject><subject>GLICOLIPIDOS</subject><subject>GLICOPROTEINAS</subject><subject>Glucan Endo-1,3-beta-D-Glucosidase - pharmacology</subject><subject>GLYCOLIPIDE</subject><subject>GLYCOPROTEINE</subject><subject>Haploidy</subject><subject>INOSITOL</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Microbiology</subject><subject>Mitosis</subject><subject>Morphogenesis - physiology</subject><subject>Morphology, structure, chemical composition</subject><subject>Mutagenesis, Insertional</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>Mutation</subject><subject>Mycology</subject><subject>PARED CELULAR</subject><subject>PAROI CELLULAIRE</subject><subject>Phenotype</subject><subject>Proteins</subject><subject>QUITINA</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Spores, Fungal - growth & development</subject><subject>STRUCTURE CELLULAIRE</subject><issn>0021-9193</issn><issn>1098-5530</issn><issn>1067-8832</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkd2K1DAYhoso67h6A4JYRTxrzU_TJAceyKLrwoIL6x6Hr2naZmiTmnRG5kq8XVNmGFyPkvA-7_eTN8veYlRiTMSnbVNizkpeYsFlgYVgJZaSPsk2GElRMEbR02yDEMGFxJI-z17EuEUIVxUjF9mFqJgQFG-yP3fDIVo_-t5qGHNwMKZ3zH2XT7sF3BJz69qkLWa97f24N5Nxywosg8nvQesBgp8OOgHaBLO30YLJr-9uCnB68MG0-Rz8YqzL-xljlsrkkw_z4HvjzNoMXJus45hHM0OAxXr3MnvWwRjNq9N5mT18-_rz6ntx--P65urLbaHrmi4FBam5EYShRkpJWo1qygWVEglkKG854bpt088w1grEQLeyMZwI1HU1agiml9nnY91510ym1Wm1AKOag50gHJQHqx4rzg6q93tFUEUqmfwfT_7gf-1MXNRk47oLOON3UeG6YmkynsD3_4Fbvwvpu6MihKM0dFUniB8hHXyMwXTnQTBSa-5q26iUu-JqzV2tuas19-R88-8eZ98p6KR_OOkQU9BdSNnYeMYqjiSVK_buiA22H37bYBTE6XHTxLw-Mh14BX1IZR7uZYWpSBv8BdlszU4</recordid><startdate>19930401</startdate><enddate>19930401</enddate><creator>Popolo, L. (Universita degli Studi di Milano, Milan, Italy)</creator><creator>Vai, M</creator><creator>Gatti, E</creator><creator>Porello, S</creator><creator>Bonfante, P</creator><creator>Balestrini, R</creator><creator>Alberghina, L</creator><general>American Society for Microbiology</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19930401</creationdate><title>Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation</title><author>Popolo, L. (Universita degli Studi di Milano, Milan, Italy) ; Vai, M ; Gatti, E ; Porello, S ; Bonfante, P ; Balestrini, R ; Alberghina, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c663t-3a9c7e8250b9992dc06378399080e37d727cdd19955d805acd9be7280ff60b213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Bacteriology</topic><topic>BIOCHIMIE</topic><topic>Biological and medical sciences</topic><topic>BIOQUIMICA</topic><topic>Cell Division - physiology</topic><topic>Cell Wall - chemistry</topic><topic>Cellular biology</topic><topic>CHITINE</topic><topic>Conjugation, Genetic</topic><topic>DIFERENCIACION CELULAR</topic><topic>DIFFERENCIATION CELLULAIRE</topic><topic>Diploidy</topic><topic>DIVISION CELLULAIRE</topic><topic>DIVISION CELULAR</topic><topic>ESTRUCTURA CELULAR</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>G1 Phase</topic><topic>G2 Phase</topic><topic>GENE</topic><topic>GENES</topic><topic>Genes, Fungal - genetics</topic><topic>GLICOLIPIDOS</topic><topic>GLICOPROTEINAS</topic><topic>Glucan Endo-1,3-beta-D-Glucosidase - pharmacology</topic><topic>GLYCOLIPIDE</topic><topic>GLYCOPROTEINE</topic><topic>Haploidy</topic><topic>INOSITOL</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Microbiology</topic><topic>Mitosis</topic><topic>Morphogenesis - physiology</topic><topic>Morphology, structure, chemical composition</topic><topic>Mutagenesis, Insertional</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>Mutation</topic><topic>Mycology</topic><topic>PARED CELULAR</topic><topic>PAROI CELLULAIRE</topic><topic>Phenotype</topic><topic>Proteins</topic><topic>QUITINA</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae - ultrastructure</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Spores, Fungal - growth & development</topic><topic>STRUCTURE CELLULAIRE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Popolo, L. (Universita degli Studi di Milano, Milan, Italy)</creatorcontrib><creatorcontrib>Vai, M</creatorcontrib><creatorcontrib>Gatti, E</creatorcontrib><creatorcontrib>Porello, S</creatorcontrib><creatorcontrib>Bonfante, P</creatorcontrib><creatorcontrib>Balestrini, R</creatorcontrib><creatorcontrib>Alberghina, L</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Popolo, L. (Universita degli Studi di Milano, Milan, Italy)</au><au>Vai, M</au><au>Gatti, E</au><au>Porello, S</au><au>Bonfante, P</au><au>Balestrini, R</au><au>Alberghina, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation</atitle><jtitle>Journal of Bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>1993-04-01</date><risdate>1993</risdate><volume>175</volume><issue>7</issue><spage>1879</spage><epage>1885</epage><pages>1879-1885</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><eissn>1067-8832</eissn><coden>JOBAAY</coden><abstract>This paper reports a phenotypic characterization of ggp1 mutants. The cloned GGP1 (GAS1) gene, which encodes a major GPI-anchored glycoprotein (gp115) of Saccharomyces cerevisiae of unknown function, was used to direct the inactivation of the chromosomal gene in haploid and diploid strains by gene replacement. The analysis of the null mutants reveals a reduction in the growth rate of 15 to 40%. Cells are round, with more than one bud, and extensively vacuolized. In the stationary phase, mutant cells are very large, arrest with a high percentage of budded cells (about 54 and 70% for haploid and diploid null mutants, respectively, in comparison with about 10 to 13% for control cells), and have reduced viability. The observed phenotype suggests defects in cell separation. Flow cytometric analysis of DNA reveals an increase in the fraction of cells in the G2+M+G1 compartment during exponential growth. Conjugation and sporulation are not affected. The exocellular location of gp115 led us to examine cell wall properties. Cell wall and septum ultrastructure of abnormally budded cells was analyzed by electron microscopy analysis, and no appreciable differences from wild-type cells were found. Microscopic analysis revealed an increase in chitin content and delocalization. In comparison with control cells, ggp1 null mutants are shown to be resistant to Zymolyase during the exponential growth phase. A fivefold overexpression of gp115 does not bring about any effects on cell growth parameters and cell wall properties</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>8458831</pmid><doi>10.1128/jb.175.7.1879-1885.1993</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of Bacteriology, 1993-04, Vol.175 (7), p.1879-1885 |
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| subjects | Bacteriology BIOCHIMIE Biological and medical sciences BIOQUIMICA Cell Division - physiology Cell Wall - chemistry Cellular biology CHITINE Conjugation, Genetic DIFERENCIACION CELULAR DIFFERENCIATION CELLULAIRE Diploidy DIVISION CELLULAIRE DIVISION CELULAR ESTRUCTURA CELULAR Fundamental and applied biological sciences. Psychology G1 Phase G2 Phase GENE GENES Genes, Fungal - genetics GLICOLIPIDOS GLICOPROTEINAS Glucan Endo-1,3-beta-D-Glucosidase - pharmacology GLYCOLIPIDE GLYCOPROTEINE Haploidy INOSITOL Membrane Glycoproteins - genetics Microbiology Mitosis Morphogenesis - physiology Morphology, structure, chemical composition Mutagenesis, Insertional MUTANT MUTANTES Mutation Mycology PARED CELULAR PAROI CELLULAIRE Phenotype Proteins QUITINA SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins Spores, Fungal - growth & development STRUCTURE CELLULAIRE |
| title | Physiological analysis of mutants indicates involvement of the Saccharomyces cerevisiae GPI-anchored protein gp115 in morphogenesis and cell separation |
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