The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis
A derivative of the α-amylase from Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteol...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1998-07, Vol.430 (3), p.385-389 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 389 |
|---|---|
| container_issue | 3 |
| container_start_page | 385 |
| container_title | FEBS letters |
| container_volume | 430 |
| creator | Stephenson, Keith Carter, Noel M Harwood, Colin R Petit-Glatron, Marie-Françoise Chambert, Régis |
| description | A derivative of the α-amylase from
Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by
Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteolysis during or shortly after translocation through the cytoplasmic membrane. When we compared the overall rate of folding of the engineered derivative (AmyLQS50.5) with that of AmyL it exhibited a greater dependency on Ca
2+ ions for in vitro folding. When the concentration of Ca
2+ in the growth medium was increased, so too did the relative yield of AmyLQS50.5. We discuss the importance of secretory protein folding at the membrane/cell wall interface with respect to the yield of native and heterologous proteins from
B. subtilis. |
| doi_str_mv | 10.1016/S0014-5793(98)00698-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80045424</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S001457939800698X</els_id><sourcerecordid>80045424</sourcerecordid><originalsourceid>FETCH-LOGICAL-c472X-70e714431a2bb333978e82a96707594b73bbdc7093d9364d4dba93baa55d761b3</originalsourceid><addsrcrecordid>eNqNkc1u1DAUhS1UVKaFR6jkVVUWKXbsxPYK0ao_SJVYUKTZWf65KUZO0tpJ0TwWL8Iz1ZkZdQsry_c7597rY4ROKDmnhLafvhNCedUIxc6U_EhIq2S1foNWVApWMd7KA7R6lbxDRzn_IuUuqTpEh6qVshHtCnX3PwGHoYszDA7w2OHHNE4QBtyN0YfhAY8DjmYCnCfzAHlRTMWSwSWYQoGl8PdPZfpNNLnwLo09vjAuxDhnnGc7hRjye_S2MzHDh_15jH5cX91f3lZ3326-Xn65qxwX9boSBATlnFFTW8sYU0KCrI1qBRGN4lYwa70TRDGvWMs999YoZo1pGi9aatkxOt31La94miFPug_ZQYxmgHHOWhLCG17zImx2QpfGnBN0-jGF3qSNpkQv-eptvnoJTyupt_nqdfGd7AfMtgf_6toHWvjtjv8OETb_11RfX13UW7IAJbflZdTnXSsogT0HSDq7sPySDwncpP0Y_rHsC13ZoAM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>80045424</pqid></control><display><type>article</type><title>The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Stephenson, Keith ; Carter, Noel M ; Harwood, Colin R ; Petit-Glatron, Marie-Françoise ; Chambert, Régis</creator><creatorcontrib>Stephenson, Keith ; Carter, Noel M ; Harwood, Colin R ; Petit-Glatron, Marie-Françoise ; Chambert, Régis</creatorcontrib><description>A derivative of the α-amylase from
Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by
Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteolysis during or shortly after translocation through the cytoplasmic membrane. When we compared the overall rate of folding of the engineered derivative (AmyLQS50.5) with that of AmyL it exhibited a greater dependency on Ca
2+ ions for in vitro folding. When the concentration of Ca
2+ in the growth medium was increased, so too did the relative yield of AmyLQS50.5. We discuss the importance of secretory protein folding at the membrane/cell wall interface with respect to the yield of native and heterologous proteins from
B. subtilis.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)00698-X</identifier><identifier>PMID: 9688576</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>alpha-Amylases - chemistry ; alpha-Amylases - metabolism ; Bacillus - enzymology ; Bacillus subtilis - enzymology ; Calcium - metabolism ; Calcium Chloride - metabolism ; Calcium ion ; Cell Membrane - enzymology ; Cell wall ; Cell Wall - enzymology ; Culture Media ; Folding ; Kinetics ; Protein Denaturation ; Protein Folding ; Protein secretion ; Recombinant Fusion Proteins</subject><ispartof>FEBS letters, 1998-07, Vol.430 (3), p.385-389</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 430 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472X-70e714431a2bb333978e82a96707594b73bbdc7093d9364d4dba93baa55d761b3</citedby><cites>FETCH-LOGICAL-c472X-70e714431a2bb333978e82a96707594b73bbdc7093d9364d4dba93baa55d761b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2900698-X$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S001457939800698X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9688576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stephenson, Keith</creatorcontrib><creatorcontrib>Carter, Noel M</creatorcontrib><creatorcontrib>Harwood, Colin R</creatorcontrib><creatorcontrib>Petit-Glatron, Marie-Françoise</creatorcontrib><creatorcontrib>Chambert, Régis</creatorcontrib><title>The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A derivative of the α-amylase from
Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by
Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteolysis during or shortly after translocation through the cytoplasmic membrane. When we compared the overall rate of folding of the engineered derivative (AmyLQS50.5) with that of AmyL it exhibited a greater dependency on Ca
2+ ions for in vitro folding. When the concentration of Ca
2+ in the growth medium was increased, so too did the relative yield of AmyLQS50.5. We discuss the importance of secretory protein folding at the membrane/cell wall interface with respect to the yield of native and heterologous proteins from
B. subtilis.</description><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - metabolism</subject><subject>Bacillus - enzymology</subject><subject>Bacillus subtilis - enzymology</subject><subject>Calcium - metabolism</subject><subject>Calcium Chloride - metabolism</subject><subject>Calcium ion</subject><subject>Cell Membrane - enzymology</subject><subject>Cell wall</subject><subject>Cell Wall - enzymology</subject><subject>Culture Media</subject><subject>Folding</subject><subject>Kinetics</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Protein secretion</subject><subject>Recombinant Fusion Proteins</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUhS1UVKaFR6jkVVUWKXbsxPYK0ao_SJVYUKTZWf65KUZO0tpJ0TwWL8Iz1ZkZdQsry_c7597rY4ROKDmnhLafvhNCedUIxc6U_EhIq2S1foNWVApWMd7KA7R6lbxDRzn_IuUuqTpEh6qVshHtCnX3PwGHoYszDA7w2OHHNE4QBtyN0YfhAY8DjmYCnCfzAHlRTMWSwSWYQoGl8PdPZfpNNLnwLo09vjAuxDhnnGc7hRjye_S2MzHDh_15jH5cX91f3lZ3326-Xn65qxwX9boSBATlnFFTW8sYU0KCrI1qBRGN4lYwa70TRDGvWMs999YoZo1pGi9aatkxOt31La94miFPug_ZQYxmgHHOWhLCG17zImx2QpfGnBN0-jGF3qSNpkQv-eptvnoJTyupt_nqdfGd7AfMtgf_6toHWvjtjv8OETb_11RfX13UW7IAJbflZdTnXSsogT0HSDq7sPySDwncpP0Y_rHsC13ZoAM</recordid><startdate>19980703</startdate><enddate>19980703</enddate><creator>Stephenson, Keith</creator><creator>Carter, Noel M</creator><creator>Harwood, Colin R</creator><creator>Petit-Glatron, Marie-Françoise</creator><creator>Chambert, Régis</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>19980703</creationdate><title>The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis</title><author>Stephenson, Keith ; Carter, Noel M ; Harwood, Colin R ; Petit-Glatron, Marie-Françoise ; Chambert, Régis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472X-70e714431a2bb333978e82a96707594b73bbdc7093d9364d4dba93baa55d761b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>alpha-Amylases - chemistry</topic><topic>alpha-Amylases - metabolism</topic><topic>Bacillus - enzymology</topic><topic>Bacillus subtilis - enzymology</topic><topic>Calcium - metabolism</topic><topic>Calcium Chloride - metabolism</topic><topic>Calcium ion</topic><topic>Cell Membrane - enzymology</topic><topic>Cell wall</topic><topic>Cell Wall - enzymology</topic><topic>Culture Media</topic><topic>Folding</topic><topic>Kinetics</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Protein secretion</topic><topic>Recombinant Fusion Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stephenson, Keith</creatorcontrib><creatorcontrib>Carter, Noel M</creatorcontrib><creatorcontrib>Harwood, Colin R</creatorcontrib><creatorcontrib>Petit-Glatron, Marie-Françoise</creatorcontrib><creatorcontrib>Chambert, Régis</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stephenson, Keith</au><au>Carter, Noel M</au><au>Harwood, Colin R</au><au>Petit-Glatron, Marie-Françoise</au><au>Chambert, Régis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-07-03</date><risdate>1998</risdate><volume>430</volume><issue>3</issue><spage>385</spage><epage>389</epage><pages>385-389</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A derivative of the α-amylase from
Bacillus licheniformis (AmyL) engineered to give an active enzyme with increased net positive charge is secreted by
Bacillus subtilis with a yield that is significantly lower than that of the native enzyme. This reduction in yield is the result of increased proteolysis during or shortly after translocation through the cytoplasmic membrane. When we compared the overall rate of folding of the engineered derivative (AmyLQS50.5) with that of AmyL it exhibited a greater dependency on Ca
2+ ions for in vitro folding. When the concentration of Ca
2+ in the growth medium was increased, so too did the relative yield of AmyLQS50.5. We discuss the importance of secretory protein folding at the membrane/cell wall interface with respect to the yield of native and heterologous proteins from
B. subtilis.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9688576</pmid><doi>10.1016/S0014-5793(98)00698-X</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1998-07, Vol.430 (3), p.385-389 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80045424 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | alpha-Amylases - chemistry alpha-Amylases - metabolism Bacillus - enzymology Bacillus subtilis - enzymology Calcium - metabolism Calcium Chloride - metabolism Calcium ion Cell Membrane - enzymology Cell wall Cell Wall - enzymology Culture Media Folding Kinetics Protein Denaturation Protein Folding Protein secretion Recombinant Fusion Proteins |
| title | The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-13T02%3A08%3A43IST&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=The%20influence%20of%20protein%20folding%20on%20late%20stages%20of%20the%20secretion%20of%20%CE%B1-amylases%20from%20Bacillus%20subtilis&rft.jtitle=FEBS%20letters&rft.au=Stephenson,%20Keith&rft.date=1998-07-03&rft.volume=430&rft.issue=3&rft.spage=385&rft.epage=389&rft.pages=385-389&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/S0014-5793(98)00698-X&rft_dat=%3Cproquest_cross%3E80045424%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=80045424&rft_id=info:pmid/9688576&rft_els_id=S001457939800698X&rfr_iscdi=true |