Protein quality control in the bacterial periplasm
<p>Abstract</p> <p>The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in <it>Escherichia coli </it>are initially synthesized in the cytoplasm, then follow a pathway that...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2004-05-01
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| Series: | Microbial Cell Factories |
| Online Access: | http://www.microbialcellfactories.com/content/3/1/4 |
| _version_ | 1819045009195794432 |
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| author | Betton Jean-Michel Miot Marika |
| author_facet | Betton Jean-Michel Miot Marika |
| author_sort | Betton Jean-Michel |
| collection | DOAJ |
| description | <p>Abstract</p> <p>The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in <it>Escherichia coli </it>are initially synthesized in the cytoplasm, then follow a pathway that depends upon their ultimate cellular destination. Many proteins destined for the periplasm are synthesized as precursors carrying an N-terminal signal sequence that directs them to the general secretion machinery at the inner membrane. After translocation and signal sequence cleavage, the newly exported mature proteins are folded and assembled in the periplasm. Maintaining quality control over these processes depends on chaperones, folding catalysts, and proteases. This article summarizes the general principles which control protein folding in the bacterial periplasm by focusing on the periplasmic maltose-binding protein.</p> |
| first_indexed | 2024-12-21T10:21:45Z |
| format | Article |
| id | doaj.art-d0c70669c25d4263afed52d528c0f580 |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-12-21T10:21:45Z |
| publishDate | 2004-05-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-d0c70669c25d4263afed52d528c0f5802022-12-21T19:07:25ZengBMCMicrobial Cell Factories1475-28592004-05-0131410.1186/1475-2859-3-4Protein quality control in the bacterial periplasmBetton Jean-MichelMiot Marika<p>Abstract</p> <p>The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in <it>Escherichia coli </it>are initially synthesized in the cytoplasm, then follow a pathway that depends upon their ultimate cellular destination. Many proteins destined for the periplasm are synthesized as precursors carrying an N-terminal signal sequence that directs them to the general secretion machinery at the inner membrane. After translocation and signal sequence cleavage, the newly exported mature proteins are folded and assembled in the periplasm. Maintaining quality control over these processes depends on chaperones, folding catalysts, and proteases. This article summarizes the general principles which control protein folding in the bacterial periplasm by focusing on the periplasmic maltose-binding protein.</p>http://www.microbialcellfactories.com/content/3/1/4 |
| spellingShingle | Betton Jean-Michel Miot Marika Protein quality control in the bacterial periplasm Microbial Cell Factories |
| title | Protein quality control in the bacterial periplasm |
| title_full | Protein quality control in the bacterial periplasm |
| title_fullStr | Protein quality control in the bacterial periplasm |
| title_full_unstemmed | Protein quality control in the bacterial periplasm |
| title_short | Protein quality control in the bacterial periplasm |
| title_sort | protein quality control in the bacterial periplasm |
| url | http://www.microbialcellfactories.com/content/3/1/4 |
| work_keys_str_mv | AT bettonjeanmichel proteinqualitycontrolinthebacterialperiplasm AT miotmarika proteinqualitycontrolinthebacterialperiplasm |