| Computational and experimental evidence for the evolution of a (beta alpha)8-barrel protein from an ancestral quarter-barrel stabilised by disulfide bonds. | |
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MedLine Citation:
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PMID: 20363228 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The evolution of the prototypical (beta alpha)(8)-barrel protein imidazole glycerol phosphate synthase (HisF) was studied by complementary computational and experimental approaches. The 4-fold symmetry of HisF suggested that its constituting (beta alpha)(2) quarter-barrels have a common evolutionary origin. This conclusion was supported by the computational reconstruction of the HisF sequence of the last common ancestor, which showed that its quarter-barrels were more similar to each other than are those of extant HisF proteins. A comprehensive sequence analysis identified HisF-N1 [corresponding to (beta alpha)(1-2)] as the slowest evolving quarter-barrel. This finding indicated that it is the closest relative of the common (beta alpha)(2) predecessor, which must have been a stable and presumably tetrameric protein. In accordance with this prediction, a recombinantly produced HisF-N1 protein was properly folded and formed a tetramer being stabilised by disulfide bonds. The introduction of a disulfide bond in HisF-C1 [corresponding to (beta alpha)(5-6)] also resulted in the formation of a stable tetramer. The fusion of two identical HisF-N1 quarter-barrels yielded the stable dimeric half-barrel HisF-N1N1. Our findings suggest a two-step evolutionary pathway in which a HisF-N1-like predecessor was duplicated and fused twice to yield HisF. Most likely, the (beta alpha)(2) quarter-barrel and (beta alpha)(4) half-barrel intermediates on this pathway were stabilised by disulfide bonds that became dispensable upon consolidation of the (beta alpha)(8)-barrel. |
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Authors:
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Markus Richter; Manal Bosnali; Linn Carstensen; Tobias Seitz; Helmut Durchschlag; Samuel Blanquart; Rainer Merkl; Reinhard Sterner |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-04-02 |
Journal Detail:
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Title: Journal of molecular biology Volume: 398 ISSN: 1089-8638 ISO Abbreviation: J. Mol. Biol. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-05-07 Completed Date: 2010-05-18 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985088R Medline TA: J Mol Biol Country: England |
Other Details:
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Languages: eng Pagination: 763-73 Citation Subset: IM |
Copyright Information:
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(c) 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universit?tsstrasse 31, D-93053 Regensburg, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Aminohydrolases
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chemistry*,
genetics*,
metabolism Bacterial Proteins / chemistry*, genetics*, metabolism Computational Biology Disulfides Evolution, Molecular* Models, Molecular Protein Folding* Recombinant Proteins / chemistry, genetics, metabolism Thermotoga maritima / enzymology* |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Disulfides; 0/Recombinant Proteins; EC 3.5.1.-/imidazole glycerol phosphate synthase; EC 3.5.4.-/Aminohydrolases |
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