Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability.
The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3352829?pdf=render |
| _version_ | 1811205752068505600 |
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| author | Kris Pauwels Manuel M Sanchez del Pino Georges Feller Patrick Van Gelder |
| author_facet | Kris Pauwels Manuel M Sanchez del Pino Georges Feller Patrick Van Gelder |
| author_sort | Kris Pauwels |
| collection | DOAJ |
| description | The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of α-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of distinct folding intermediates, we demonstrate that the native lipase has a kinetically stable conformation. We show that a newly discovered molten globule-like conformation has distinct properties that clearly differ from those of the near-native intermediate state. The folding fingerprint of Lif-dependent lipases is put in the context of the protease-prodomain system and the comparison reveals clear differences that render the lipase-Lif systems unique. Limited proteolysis unveils structural differences between the near-native intermediate and the native conformation and sets the stage to shed light onto the nature of the kinetic barrier. |
| first_indexed | 2024-04-12T03:36:42Z |
| format | Article |
| id | doaj.art-76f7abacca374a66a2ac73486ac92f7c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-12T03:36:42Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-76f7abacca374a66a2ac73486ac92f7c2022-12-22T03:49:24ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0175e3699910.1371/journal.pone.0036999Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability.Kris PauwelsManuel M Sanchez del PinoGeorges FellerPatrick Van GelderThe lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of α-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of distinct folding intermediates, we demonstrate that the native lipase has a kinetically stable conformation. We show that a newly discovered molten globule-like conformation has distinct properties that clearly differ from those of the near-native intermediate state. The folding fingerprint of Lif-dependent lipases is put in the context of the protease-prodomain system and the comparison reveals clear differences that render the lipase-Lif systems unique. Limited proteolysis unveils structural differences between the near-native intermediate and the native conformation and sets the stage to shed light onto the nature of the kinetic barrier.http://europepmc.org/articles/PMC3352829?pdf=render |
| spellingShingle | Kris Pauwels Manuel M Sanchez del Pino Georges Feller Patrick Van Gelder Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. PLoS ONE |
| title | Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. |
| title_full | Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. |
| title_fullStr | Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. |
| title_full_unstemmed | Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. |
| title_short | Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stability. |
| title_sort | decoding the folding of burkholderia glumae lipase folding intermediates en route to kinetic stability |
| url | http://europepmc.org/articles/PMC3352829?pdf=render |
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