Polypeptide translocation by the AAA+ ClpXP protease machine
In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite m...
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| Format: | Article |
| Language: | en_US |
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Elsevier
2012
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| Online Access: | http://hdl.handle.net/1721.1/72391 https://orcid.org/0000-0002-1719-5399 |
| _version_ | 1811078395955511296 |
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| author | Barkow, Sarah R. Levchenko, Igor Baker, Tania Sauer, Robert T |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Barkow, Sarah R. Levchenko, Igor Baker, Tania Sauer, Robert T |
| author_sort | Barkow, Sarah R. |
| collection | MIT |
| description | In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and polarity. Moreover, translocation occurs without a peptide –NH and with 10 methylenes between successive peptide bonds. Pulling on homopolymeric tracts of glycine, proline, and lysine also allows efficient ClpXP degradation of a stably folded protein. Thus, minimal chemical features of a polypeptide chain are sufficient for translocation and protein unfolding by the ClpX machine. These results suggest that the translocation pore of ClpX is highly elastic, allowing interactions with a wide range of chemical groups, a feature likely to be shared by many AAA+ unfoldases. |
| first_indexed | 2024-09-23T10:58:50Z |
| format | Article |
| id | mit-1721.1/72391 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T10:58:50Z |
| publishDate | 2012 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/723912024-03-21T20:14:33Z Polypeptide translocation by the AAA+ ClpXP protease machine Barkow, Sarah R. Levchenko, Igor Baker, Tania Sauer, Robert T Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Baker, Tania Barkow, Sarah R. Levchenko, Igor Baker, Tania Sauer, Robert T. In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and polarity. Moreover, translocation occurs without a peptide –NH and with 10 methylenes between successive peptide bonds. Pulling on homopolymeric tracts of glycine, proline, and lysine also allows efficient ClpXP degradation of a stably folded protein. Thus, minimal chemical features of a polypeptide chain are sufficient for translocation and protein unfolding by the ClpX machine. These results suggest that the translocation pore of ClpX is highly elastic, allowing interactions with a wide range of chemical groups, a feature likely to be shared by many AAA+ unfoldases. National Institutes of Health (U.S.) (AI-15706) 2012-08-28T19:49:58Z 2012-08-28T19:49:58Z 2009-06 2009-04 Article http://purl.org/eprint/type/JournalArticle 1074-5521 http://hdl.handle.net/1721.1/72391 Barkow, Sarah R. et al. “Polypeptide Translocation by the AAA+ ClpXP Protease Machine.” Chemistry & Biology 16.6 (2009): 605–612. https://orcid.org/0000-0002-1719-5399 en_US http://dx.doi.org/10.1016/j.chembiol.2009.05.007 Chemistry and Biology Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Elsevier PMC |
| spellingShingle | Barkow, Sarah R. Levchenko, Igor Baker, Tania Sauer, Robert T Polypeptide translocation by the AAA+ ClpXP protease machine |
| title | Polypeptide translocation by the AAA+ ClpXP protease machine |
| title_full | Polypeptide translocation by the AAA+ ClpXP protease machine |
| title_fullStr | Polypeptide translocation by the AAA+ ClpXP protease machine |
| title_full_unstemmed | Polypeptide translocation by the AAA+ ClpXP protease machine |
| title_short | Polypeptide translocation by the AAA+ ClpXP protease machine |
| title_sort | polypeptide translocation by the aaa clpxp protease machine |
| url | http://hdl.handle.net/1721.1/72391 https://orcid.org/0000-0002-1719-5399 |
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