Loading…
Export of an invertase by yeast Candida utilis cells
Export and accumulation of various forms of invertase (EC 3.2.1.26) in the cell wall and culture medium of the yeast Candida utilis was investigated. It was found that there is the high-molecular-weight invertase in the cell wall (CW-form). This form is not exported into the culture medium, and it i...
Saved in:
Published in: | Applied biochemistry and microbiology 2014-03, Vol.50 (2), p.134-139 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883 |
---|---|
cites | cdi_FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883 |
container_end_page | 139 |
container_issue | 2 |
container_start_page | 134 |
container_title | Applied biochemistry and microbiology |
container_volume | 50 |
creator | Alekseeva, O. V Sabirzyanova, T. A Selyah, I. O Kalebina, T. S Kulaev, I. S |
description | Export and accumulation of various forms of invertase (EC 3.2.1.26) in the cell wall and culture medium of the yeast Candida utilis was investigated. It was found that there is the high-molecular-weight invertase in the cell wall (CW-form). This form is not exported into the culture medium, and it is by a third more glycosylated than the previously described exported S-form. It was shown that one of the two forms of invertase exported into the culture medium—the glycosylated S-form—is retained in the cell wall, while the other one-the nonglycosylated F-form—was not detected in the cell wall. Based on these results, as well as data on the distribution dynamics of the enzyme in the culture medium and in the cell wall during different growth stages of a yeast culture, we suggested that the nonglycosylated form was exported into the culture medium via the zone of abnormal cell wall permeability and the glycosylated forms of this enzyme (both exported and nonexported) did not use this pathway and the degree of N-glycosylation is an important factor determining the final localization of the enzyme. |
doi_str_mv | 10.1134/S0003683814020033 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1508758291</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1508758291</sourcerecordid><originalsourceid>FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883</originalsourceid><addsrcrecordid>eNp9kE9Lw0AQxRdRsFY_gCcXvHiJ7uy_bI5SWhUKHmrPyybdlJQ0qTuJ2G_vhngQBS-zs7zfewyPkGtg9wBCPqwYY0IbYUAyHldxQiagmUkE4_KUTAY5GfRzcoG4i99Mm2xC5Pzz0IaOtiV1Da2aDx86h57mR3r0Djs6c82m2jjad1VdIS18XeMlOStdjf7q-52S9WL-NntOlq9PL7PHZVKIVHRJkaeiKLksmCqEA-9AOqW5UR6YykXKc4Bc-lxvpNEZz9PSS6EA4jCQGiOm5G7MPYT2vffY2X2FwwWu8W2PFhQzqTI8g4je_kJ3bR-aeN1AxcRMCx4pGKkitIjBl_YQqr0LRwvMDj3aPz1GDx89GNlm68OP5H9MN6OpdK1121ChXa84i3osPksj8gXVL3oE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1504359632</pqid></control><display><type>article</type><title>Export of an invertase by yeast Candida utilis cells</title><source>Springer Link</source><creator>Alekseeva, O. V ; Sabirzyanova, T. A ; Selyah, I. O ; Kalebina, T. S ; Kulaev, I. S</creator><creatorcontrib>Alekseeva, O. V ; Sabirzyanova, T. A ; Selyah, I. O ; Kalebina, T. S ; Kulaev, I. S</creatorcontrib><description>Export and accumulation of various forms of invertase (EC 3.2.1.26) in the cell wall and culture medium of the yeast Candida utilis was investigated. It was found that there is the high-molecular-weight invertase in the cell wall (CW-form). This form is not exported into the culture medium, and it is by a third more glycosylated than the previously described exported S-form. It was shown that one of the two forms of invertase exported into the culture medium—the glycosylated S-form—is retained in the cell wall, while the other one-the nonglycosylated F-form—was not detected in the cell wall. Based on these results, as well as data on the distribution dynamics of the enzyme in the culture medium and in the cell wall during different growth stages of a yeast culture, we suggested that the nonglycosylated form was exported into the culture medium via the zone of abnormal cell wall permeability and the glycosylated forms of this enzyme (both exported and nonexported) did not use this pathway and the degree of N-glycosylation is an important factor determining the final localization of the enzyme.</description><identifier>ISSN: 0003-6838</identifier><identifier>EISSN: 1608-3024</identifier><identifier>DOI: 10.1134/S0003683814020033</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>beta-fructofuranosidase ; Biochemistry ; Biomedical and Life Sciences ; Candida utilis ; cell walls ; Cellular biology ; culture media ; developmental stages ; Enzymes ; Life Sciences ; Medical Microbiology ; Microbiology ; Yeast ; Yeasts</subject><ispartof>Applied biochemistry and microbiology, 2014-03, Vol.50 (2), p.134-139</ispartof><rights>Pleiades Publishing, Inc. 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883</citedby><cites>FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Alekseeva, O. V</creatorcontrib><creatorcontrib>Sabirzyanova, T. A</creatorcontrib><creatorcontrib>Selyah, I. O</creatorcontrib><creatorcontrib>Kalebina, T. S</creatorcontrib><creatorcontrib>Kulaev, I. S</creatorcontrib><title>Export of an invertase by yeast Candida utilis cells</title><title>Applied biochemistry and microbiology</title><addtitle>Appl Biochem Microbiol</addtitle><description>Export and accumulation of various forms of invertase (EC 3.2.1.26) in the cell wall and culture medium of the yeast Candida utilis was investigated. It was found that there is the high-molecular-weight invertase in the cell wall (CW-form). This form is not exported into the culture medium, and it is by a third more glycosylated than the previously described exported S-form. It was shown that one of the two forms of invertase exported into the culture medium—the glycosylated S-form—is retained in the cell wall, while the other one-the nonglycosylated F-form—was not detected in the cell wall. Based on these results, as well as data on the distribution dynamics of the enzyme in the culture medium and in the cell wall during different growth stages of a yeast culture, we suggested that the nonglycosylated form was exported into the culture medium via the zone of abnormal cell wall permeability and the glycosylated forms of this enzyme (both exported and nonexported) did not use this pathway and the degree of N-glycosylation is an important factor determining the final localization of the enzyme.</description><subject>beta-fructofuranosidase</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Candida utilis</subject><subject>cell walls</subject><subject>Cellular biology</subject><subject>culture media</subject><subject>developmental stages</subject><subject>Enzymes</subject><subject>Life Sciences</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0003-6838</issn><issn>1608-3024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNp9kE9Lw0AQxRdRsFY_gCcXvHiJ7uy_bI5SWhUKHmrPyybdlJQ0qTuJ2G_vhngQBS-zs7zfewyPkGtg9wBCPqwYY0IbYUAyHldxQiagmUkE4_KUTAY5GfRzcoG4i99Mm2xC5Pzz0IaOtiV1Da2aDx86h57mR3r0Djs6c82m2jjad1VdIS18XeMlOStdjf7q-52S9WL-NntOlq9PL7PHZVKIVHRJkaeiKLksmCqEA-9AOqW5UR6YykXKc4Bc-lxvpNEZz9PSS6EA4jCQGiOm5G7MPYT2vffY2X2FwwWu8W2PFhQzqTI8g4je_kJ3bR-aeN1AxcRMCx4pGKkitIjBl_YQqr0LRwvMDj3aPz1GDx89GNlm68OP5H9MN6OpdK1121ChXa84i3osPksj8gXVL3oE</recordid><startdate>20140301</startdate><enddate>20140301</enddate><creator>Alekseeva, O. V</creator><creator>Sabirzyanova, T. A</creator><creator>Selyah, I. O</creator><creator>Kalebina, T. S</creator><creator>Kulaev, I. S</creator><general>Springer-Verlag</general><general>Springer US</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20140301</creationdate><title>Export of an invertase by yeast Candida utilis cells</title><author>Alekseeva, O. V ; Sabirzyanova, T. A ; Selyah, I. O ; Kalebina, T. S ; Kulaev, I. S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>beta-fructofuranosidase</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Candida utilis</topic><topic>cell walls</topic><topic>Cellular biology</topic><topic>culture media</topic><topic>developmental stages</topic><topic>Enzymes</topic><topic>Life Sciences</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alekseeva, O. V</creatorcontrib><creatorcontrib>Sabirzyanova, T. A</creatorcontrib><creatorcontrib>Selyah, I. O</creatorcontrib><creatorcontrib>Kalebina, T. S</creatorcontrib><creatorcontrib>Kulaev, I. S</creatorcontrib><collection>AGRIS</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Applied biochemistry and microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alekseeva, O. V</au><au>Sabirzyanova, T. A</au><au>Selyah, I. O</au><au>Kalebina, T. S</au><au>Kulaev, I. S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Export of an invertase by yeast Candida utilis cells</atitle><jtitle>Applied biochemistry and microbiology</jtitle><stitle>Appl Biochem Microbiol</stitle><date>2014-03-01</date><risdate>2014</risdate><volume>50</volume><issue>2</issue><spage>134</spage><epage>139</epage><pages>134-139</pages><issn>0003-6838</issn><eissn>1608-3024</eissn><abstract>Export and accumulation of various forms of invertase (EC 3.2.1.26) in the cell wall and culture medium of the yeast Candida utilis was investigated. It was found that there is the high-molecular-weight invertase in the cell wall (CW-form). This form is not exported into the culture medium, and it is by a third more glycosylated than the previously described exported S-form. It was shown that one of the two forms of invertase exported into the culture medium—the glycosylated S-form—is retained in the cell wall, while the other one-the nonglycosylated F-form—was not detected in the cell wall. Based on these results, as well as data on the distribution dynamics of the enzyme in the culture medium and in the cell wall during different growth stages of a yeast culture, we suggested that the nonglycosylated form was exported into the culture medium via the zone of abnormal cell wall permeability and the glycosylated forms of this enzyme (both exported and nonexported) did not use this pathway and the degree of N-glycosylation is an important factor determining the final localization of the enzyme.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><doi>10.1134/S0003683814020033</doi><tpages>6</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0003-6838 |
ispartof | Applied biochemistry and microbiology, 2014-03, Vol.50 (2), p.134-139 |
issn | 0003-6838 1608-3024 |
language | eng |
recordid | cdi_proquest_miscellaneous_1508758291 |
source | Springer Link |
subjects | beta-fructofuranosidase Biochemistry Biomedical and Life Sciences Candida utilis cell walls Cellular biology culture media developmental stages Enzymes Life Sciences Medical Microbiology Microbiology Yeast Yeasts |
title | Export of an invertase by yeast Candida utilis cells |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T15%3A27%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Export%20of%20an%20invertase%20by%20yeast%20Candida%20utilis%20cells&rft.jtitle=Applied%20biochemistry%20and%20microbiology&rft.au=Alekseeva,%20O.%20V&rft.date=2014-03-01&rft.volume=50&rft.issue=2&rft.spage=134&rft.epage=139&rft.pages=134-139&rft.issn=0003-6838&rft.eissn=1608-3024&rft_id=info:doi/10.1134/S0003683814020033&rft_dat=%3Cproquest_cross%3E1508758291%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c373t-cb73cf24c05c3a1ea14a56285e105b372b11b4eb6d48692b7fe43511435817883%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1504359632&rft_id=info:pmid/&rfr_iscdi=true |