Degradation versus Aggregation of Misfolded Maltose-binding Protein in the Periplasm of Escherichia coli
The periplasmic fates of misfolded MalE31, a defective folding mutant of the maltose-binding protein, were determined by manipulating two cellular activities affecting the protein folding pathway in host cells: (i) the malEppromoter activity, which is controlled by the transcriptional activator MalT...
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| Veröffentlicht in: | The Journal of biological chemistry 1998-04, Vol.273 (15), p.8897-8902 |
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| container_title | The Journal of biological chemistry |
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| creator | Betton, Jean-Michel Sassoon, Nathalie Hofnung, Maurice Laurent, Michel |
| description | The periplasmic fates of misfolded MalE31, a defective folding mutant of the maltose-binding protein, were determined by manipulating two cellular activities affecting the protein folding pathway in host cells: (i) the malEppromoter activity, which is controlled by the transcriptional activator MalT, and (ii) the DegP and Protease III periplasmic proteolytic activity. At a low level of expression, the degradation of misfolded MalE31 was partially impaired in cells lacking DegP or Protease III. At a high level of expression, misfolded MalE31 rapidly formed periplasmic inclusion bodies and thus escaped degradation. However, the manipulated host cell activities did not enhance the production of periplasmic, soluble MalE31. A kinetic competition between folding, aggregation, and degradation is proposed as a general model for the biogenesis of periplasmic proteins. |
| doi_str_mv | 10.1074/jbc.273.15.8897 |
| format | Article |
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At a low level of expression, the degradation of misfolded MalE31 was partially impaired in cells lacking DegP or Protease III. At a high level of expression, misfolded MalE31 rapidly formed periplasmic inclusion bodies and thus escaped degradation. However, the manipulated host cell activities did not enhance the production of periplasmic, soluble MalE31. 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Sassoon, Nathalie ; Hofnung, Maurice ; Laurent, Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-79c4945ed873eca25e051d6676f07b84bb7332dabace6c58ccac988aa7cafa0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ATP-Binding Cassette Transporters</topic><topic>Bacterial Proteins - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>DNA-Binding Proteins</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>Genotype</topic><topic>Heat-Shock Proteins</topic><topic>Kinetics</topic><topic>Maltose - metabolism</topic><topic>Maltose-Binding Proteins</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Models, Chemical</topic><topic>Monosaccharide Transport Proteins</topic><topic>Mutagenesis</topic><topic>Periplasm - metabolism</topic><topic>Periplasmic Binding Proteins</topic><topic>Periplasmic Proteins</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Betton, Jean-Michel</creatorcontrib><creatorcontrib>Sassoon, Nathalie</creatorcontrib><creatorcontrib>Hofnung, Maurice</creatorcontrib><creatorcontrib>Laurent, Michel</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Betton, Jean-Michel</au><au>Sassoon, Nathalie</au><au>Hofnung, Maurice</au><au>Laurent, Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Degradation versus Aggregation of Misfolded Maltose-binding Protein in the Periplasm of Escherichia coli</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-04-10</date><risdate>1998</risdate><volume>273</volume><issue>15</issue><spage>8897</spage><epage>8902</epage><pages>8897-8902</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The periplasmic fates of misfolded MalE31, a defective folding mutant of the maltose-binding protein, were determined by manipulating two cellular activities affecting the protein folding pathway in host cells: (i) the malEppromoter activity, which is controlled by the transcriptional activator MalT, and (ii) the DegP and Protease III periplasmic proteolytic activity. 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| ispartof | The Journal of biological chemistry, 1998-04, Vol.273 (15), p.8897-8902 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | ATP-Binding Cassette Transporters Bacterial Proteins - metabolism Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism DNA-Binding Proteins Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Genotype Heat-Shock Proteins Kinetics Maltose - metabolism Maltose-Binding Proteins Metalloendopeptidases - metabolism Models, Chemical Monosaccharide Transport Proteins Mutagenesis Periplasm - metabolism Periplasmic Binding Proteins Periplasmic Proteins Promoter Regions, Genetic Protein Denaturation Protein Folding Serine Endopeptidases - metabolism Transcription Factors - metabolism |
| title | Degradation versus Aggregation of Misfolded Maltose-binding Protein in the Periplasm of Escherichia coli |
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