Genetics and molecular biology of chitin synthesis in fungi
In Saccharomyces cerevisiae, three chitin synthases have been detected. Chitin synthases I and II, the products of the CHS1 and CHS2 genes, respectively, are closely related proteins that require partial proteolysis for activity in vitro. In contrast, chitin synthase III is active in vitro without p...
Gespeichert in:
| Veröffentlicht in: | Annual review of microbiology 1993, Vol.47 (1), p.505-534 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 534 |
|---|---|
| container_issue | 1 |
| container_start_page | 505 |
| container_title | Annual review of microbiology |
| container_volume | 47 |
| creator | Bulawa, C.E |
| description | In Saccharomyces cerevisiae, three chitin synthases have been detected. Chitin synthases I and II, the products of the CHS1 and CHS2 genes, respectively, are closely related proteins that require partial proteolysis for activity in vitro. In contrast, chitin synthase III is active in vitro without protease treatment, and three genes, CSD2 (= CAL1), CSD4 (= CAL2), and CAL3, are required for its activity. In the cell, the three enzymes have different functions. Chitin synthase I and II make only a small portion, < 10%, of the cellular chitin. In acidic media, chitin synthase I is required for normal budding. Chitin synthase II is required for normal morphology, septation, and cell separation. Chitin synthase III is required for the synthesis of 90% of the cellular chitin, including the chitin in the bud scars and lateral wall. Mutants defective in chitin synthase III are resistant to Calcofluor and Kluyveromyces lactis killer toxin, they lack alkali-insoluble glucan, and under certain circumstances, they are temperature-sensitive for growth. The available data suggest that many fungi have more than one chitin synthase and that these synthases are related to the S. cerevisiae CHS and CSD gene products. |
| doi_str_mv | 10.1146/annurev.mi.47.100193.002445 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_76102578</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A15539433</galeid><sourcerecordid>A15539433</sourcerecordid><originalsourceid>FETCH-LOGICAL-c381t-65072290e089587607574c794da90305191b574fac3c61d3ac80f52e74d8bd6c3</originalsourceid><addsrcrecordid>eNptkVFr3iAUhmVsdF-7_YHBIGxjV012jBqVXpXStYNCL7pei5_R1JJop8ng-_ezJPRiFC_Ec54j73tehL5iaDCm3Q8dwpLs32byDeUNBsCSNAAtpewN2mFGWU1aht-iHUDX1bRt-Xt0nPMjAFAO8ggdiZZxDHyHzq5ssLM3udKhr6Y4WrOMOlV7H8c4HKroKvPgZx-qfAjzg80-V-XhljD4D-id02O2H7f7BN3_vPx9cV3f3F79uji_qQ0ReK47BrxtJVgQkgneAWecGi5pryUQYFjifak4bYjpcE-0EeBYazntxb7vDDlB39d_n1L8s9g8q8lnY8dRBxuXrHiHofgRBfzyH_gYlxSKNtUCE0JILgt0ukKDHq3ywcU5aTOUNSQ9xmCdL-VzzBiRlJCC16_g5fR28uY1_mzlTYo5J-vUU_KTTgeFQT3Hp7b4iglFuVrjU2t8Zfrz5mDZT7Z_md3yKv1vW19no0eXdDA-v2CEl13wZxGfVszpqPSQCnJ_V-RhQYD8A9cXq1U</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>205888979</pqid></control><display><type>article</type><title>Genetics and molecular biology of chitin synthesis in fungi</title><source>Annual Reviews Complete A-Z List</source><source>MEDLINE</source><creator>Bulawa, C.E</creator><creatorcontrib>Bulawa, C.E</creatorcontrib><description>In Saccharomyces cerevisiae, three chitin synthases have been detected. Chitin synthases I and II, the products of the CHS1 and CHS2 genes, respectively, are closely related proteins that require partial proteolysis for activity in vitro. In contrast, chitin synthase III is active in vitro without protease treatment, and three genes, CSD2 (= CAL1), CSD4 (= CAL2), and CAL3, are required for its activity. In the cell, the three enzymes have different functions. Chitin synthase I and II make only a small portion, < 10%, of the cellular chitin. In acidic media, chitin synthase I is required for normal budding. Chitin synthase II is required for normal morphology, septation, and cell separation. Chitin synthase III is required for the synthesis of 90% of the cellular chitin, including the chitin in the bud scars and lateral wall. Mutants defective in chitin synthase III are resistant to Calcofluor and Kluyveromyces lactis killer toxin, they lack alkali-insoluble glucan, and under certain circumstances, they are temperature-sensitive for growth. The available data suggest that many fungi have more than one chitin synthase and that these synthases are related to the S. cerevisiae CHS and CSD gene products.</description><identifier>ISSN: 0066-4227</identifier><identifier>EISSN: 1545-3251</identifier><identifier>DOI: 10.1146/annurev.mi.47.100193.002445</identifier><identifier>PMID: 8257107</identifier><identifier>CODEN: ARMIAZ</identifier><language>eng</language><publisher>Palo Alto, CA: Annual Reviews</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; BIOSINTESIS ; BIOSYNTHESE ; BIOSYNTHESIS ; Carbohydrate Sequence ; CELL WALLS ; Cellular biology ; CHAMPIGNON ; CHITIN ; Chitin - genetics ; Chitin - metabolism ; CHITIN SYNTHASE ; CHITINE ; Fundamental and applied biological sciences. Psychology ; FUNGI ; Fungi - genetics ; Fungi - metabolism ; Genes. Genome ; GENETICA MOLECULAR ; Genetics ; GENETIQUE MOLECULAIRE ; HONGOS ; Molecular and cellular biology ; Molecular biology ; MOLECULAR GENETICS ; Molecular Sequence Data ; Molecules ; PARED CELULAR ; PAROI CELLULAIRE ; QUITINA ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism</subject><ispartof>Annual review of microbiology, 1993, Vol.47 (1), p.505-534</ispartof><rights>1994 INIST-CNRS</rights><rights>COPYRIGHT 1993 Annual Reviews, Inc.</rights><rights>Copyright Annual Reviews, Inc. 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-65072290e089587607574c794da90305191b574fac3c61d3ac80f52e74d8bd6c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,4168,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3776173$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8257107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bulawa, C.E</creatorcontrib><title>Genetics and molecular biology of chitin synthesis in fungi</title><title>Annual review of microbiology</title><addtitle>Annu Rev Microbiol</addtitle><description>In Saccharomyces cerevisiae, three chitin synthases have been detected. Chitin synthases I and II, the products of the CHS1 and CHS2 genes, respectively, are closely related proteins that require partial proteolysis for activity in vitro. In contrast, chitin synthase III is active in vitro without protease treatment, and three genes, CSD2 (= CAL1), CSD4 (= CAL2), and CAL3, are required for its activity. In the cell, the three enzymes have different functions. Chitin synthase I and II make only a small portion, < 10%, of the cellular chitin. In acidic media, chitin synthase I is required for normal budding. Chitin synthase II is required for normal morphology, septation, and cell separation. Chitin synthase III is required for the synthesis of 90% of the cellular chitin, including the chitin in the bud scars and lateral wall. Mutants defective in chitin synthase III are resistant to Calcofluor and Kluyveromyces lactis killer toxin, they lack alkali-insoluble glucan, and under certain circumstances, they are temperature-sensitive for growth. The available data suggest that many fungi have more than one chitin synthase and that these synthases are related to the S. cerevisiae CHS and CSD gene products.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>BIOSINTESIS</subject><subject>BIOSYNTHESE</subject><subject>BIOSYNTHESIS</subject><subject>Carbohydrate Sequence</subject><subject>CELL WALLS</subject><subject>Cellular biology</subject><subject>CHAMPIGNON</subject><subject>CHITIN</subject><subject>Chitin - genetics</subject><subject>Chitin - metabolism</subject><subject>CHITIN SYNTHASE</subject><subject>CHITINE</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>FUNGI</subject><subject>Fungi - genetics</subject><subject>Fungi - metabolism</subject><subject>Genes. Genome</subject><subject>GENETICA MOLECULAR</subject><subject>Genetics</subject><subject>GENETIQUE MOLECULAIRE</subject><subject>HONGOS</subject><subject>Molecular and cellular biology</subject><subject>Molecular biology</subject><subject>MOLECULAR GENETICS</subject><subject>Molecular Sequence Data</subject><subject>Molecules</subject><subject>PARED CELULAR</subject><subject>PAROI CELLULAIRE</subject><subject>QUITINA</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><issn>0066-4227</issn><issn>1545-3251</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkVFr3iAUhmVsdF-7_YHBIGxjV012jBqVXpXStYNCL7pei5_R1JJop8ng-_ezJPRiFC_Ec54j73tehL5iaDCm3Q8dwpLs32byDeUNBsCSNAAtpewN2mFGWU1aht-iHUDX1bRt-Xt0nPMjAFAO8ggdiZZxDHyHzq5ssLM3udKhr6Y4WrOMOlV7H8c4HKroKvPgZx-qfAjzg80-V-XhljD4D-id02O2H7f7BN3_vPx9cV3f3F79uji_qQ0ReK47BrxtJVgQkgneAWecGi5pryUQYFjifak4bYjpcE-0EeBYazntxb7vDDlB39d_n1L8s9g8q8lnY8dRBxuXrHiHofgRBfzyH_gYlxSKNtUCE0JILgt0ukKDHq3ywcU5aTOUNSQ9xmCdL-VzzBiRlJCC16_g5fR28uY1_mzlTYo5J-vUU_KTTgeFQT3Hp7b4iglFuVrjU2t8Zfrz5mDZT7Z_md3yKv1vW19no0eXdDA-v2CEl13wZxGfVszpqPSQCnJ_V-RhQYD8A9cXq1U</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Bulawa, C.E</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</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>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>1993</creationdate><title>Genetics and molecular biology of chitin synthesis in fungi</title><author>Bulawa, C.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-65072290e089587607574c794da90305191b574fac3c61d3ac80f52e74d8bd6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>BIOSINTESIS</topic><topic>BIOSYNTHESE</topic><topic>BIOSYNTHESIS</topic><topic>Carbohydrate Sequence</topic><topic>CELL WALLS</topic><topic>Cellular biology</topic><topic>CHAMPIGNON</topic><topic>CHITIN</topic><topic>Chitin - genetics</topic><topic>Chitin - metabolism</topic><topic>CHITIN SYNTHASE</topic><topic>CHITINE</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>FUNGI</topic><topic>Fungi - genetics</topic><topic>Fungi - metabolism</topic><topic>Genes. Genome</topic><topic>GENETICA MOLECULAR</topic><topic>Genetics</topic><topic>GENETIQUE MOLECULAIRE</topic><topic>HONGOS</topic><topic>Molecular and cellular biology</topic><topic>Molecular biology</topic><topic>MOLECULAR GENETICS</topic><topic>Molecular Sequence Data</topic><topic>Molecules</topic><topic>PARED CELULAR</topic><topic>PAROI CELLULAIRE</topic><topic>QUITINA</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bulawa, C.E</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>Virology and AIDS Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Annual review of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bulawa, C.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetics and molecular biology of chitin synthesis in fungi</atitle><jtitle>Annual review of microbiology</jtitle><addtitle>Annu Rev Microbiol</addtitle><date>1993</date><risdate>1993</risdate><volume>47</volume><issue>1</issue><spage>505</spage><epage>534</epage><pages>505-534</pages><issn>0066-4227</issn><eissn>1545-3251</eissn><coden>ARMIAZ</coden><abstract>In Saccharomyces cerevisiae, three chitin synthases have been detected. Chitin synthases I and II, the products of the CHS1 and CHS2 genes, respectively, are closely related proteins that require partial proteolysis for activity in vitro. In contrast, chitin synthase III is active in vitro without protease treatment, and three genes, CSD2 (= CAL1), CSD4 (= CAL2), and CAL3, are required for its activity. In the cell, the three enzymes have different functions. Chitin synthase I and II make only a small portion, < 10%, of the cellular chitin. In acidic media, chitin synthase I is required for normal budding. Chitin synthase II is required for normal morphology, septation, and cell separation. Chitin synthase III is required for the synthesis of 90% of the cellular chitin, including the chitin in the bud scars and lateral wall. Mutants defective in chitin synthase III are resistant to Calcofluor and Kluyveromyces lactis killer toxin, they lack alkali-insoluble glucan, and under certain circumstances, they are temperature-sensitive for growth. The available data suggest that many fungi have more than one chitin synthase and that these synthases are related to the S. cerevisiae CHS and CSD gene products.</abstract><cop>Palo Alto, CA</cop><pub>Annual Reviews</pub><pmid>8257107</pmid><doi>10.1146/annurev.mi.47.100193.002445</doi><tpages>30</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0066-4227 |
| ispartof | Annual review of microbiology, 1993, Vol.47 (1), p.505-534 |
| issn | 0066-4227 1545-3251 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76102578 |
| source | Annual Reviews Complete A-Z List; MEDLINE |
| subjects | Amino Acid Sequence Biological and medical sciences BIOSINTESIS BIOSYNTHESE BIOSYNTHESIS Carbohydrate Sequence CELL WALLS Cellular biology CHAMPIGNON CHITIN Chitin - genetics Chitin - metabolism CHITIN SYNTHASE CHITINE Fundamental and applied biological sciences. Psychology FUNGI Fungi - genetics Fungi - metabolism Genes. Genome GENETICA MOLECULAR Genetics GENETIQUE MOLECULAIRE HONGOS Molecular and cellular biology Molecular biology MOLECULAR GENETICS Molecular Sequence Data Molecules PARED CELULAR PAROI CELLULAIRE QUITINA SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism |
| title | Genetics and molecular biology of chitin synthesis in fungi |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T06%3A22%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Genetics%20and%20molecular%20biology%20of%20chitin%20synthesis%20in%20fungi&rft.jtitle=Annual%20review%20of%20microbiology&rft.au=Bulawa,%20C.E&rft.date=1993&rft.volume=47&rft.issue=1&rft.spage=505&rft.epage=534&rft.pages=505-534&rft.issn=0066-4227&rft.eissn=1545-3251&rft.coden=ARMIAZ&rft_id=info:doi/10.1146/annurev.mi.47.100193.002445&rft_dat=%3Cgale_proqu%3EA15539433%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=205888979&rft_id=info:pmid/8257107&rft_galeid=A15539433&rfr_iscdi=true |