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http://hdl.handle.net/2445/116023
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DC Field | Value | Language |
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dc.contributor.author | Chakraborty, Arka | - |
dc.contributor.author | Lyonnais, Sébastien | - |
dc.contributor.author | Battistini, Federica | - |
dc.contributor.author | Hospital Gasch, Adam | - |
dc.contributor.author | Medici, Giorgio | - |
dc.contributor.author | Prohens López, Rafael | - |
dc.contributor.author | Orozco López, Modesto | - |
dc.contributor.author | Vilardell, Josep | - |
dc.contributor.author | Solà, Maria | - |
dc.date.accessioned | 2017-09-29T10:34:41Z | - |
dc.date.available | 2017-09-29T10:34:41Z | - |
dc.date.issued | 2016-11-28 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | http://hdl.handle.net/2445/116023 | - |
dc.description.abstract | The mitochondrial genome (mtDNA) is assembled into nucleo-protein structures termed nucleoids and maintained differently compared to nuclear DNA, the involved molecular basis remaining poorly understood. In yeast (Saccharomyces cerevisiae), mtDNA is a ∼80 kbp linear molecule and Abf2p, a double HMG-box protein, packages and maintains it. The protein binds DNA in a non-sequence-specific manner, but displays a distinct 'phased-binding' at specific DNA sequences containing poly-adenine tracts (A-tracts). We present here two crystal structures of Abf2p in complex with mtDNA-derived fragments bearing A-tracts. Each HMG-box of Abf2p induces a 90° bend in the contacted DNA, causing an overall U-turn. Together with previous data, this suggests that U-turn formation is the universal mechanism underlying mtDNA compaction induced by HMG-box proteins. Combining this structural information with mutational, biophysical and computational analyses, we reveal a unique DNA binding mechanism for Abf2p where a characteristic N-terminal flag and helix are crucial for mtDNA maintenance. Additionally, we provide the molecular basis for A-tract mediated exclusion of Abf2p binding. Due to high prevalence of A-tracts in yeast mtDNA, this has critical relevance for nucleoid architecture. Therefore, an unprecedented A-tract mediated protein positioning mechanism regulates DNA packaging proteins in the mitochondria, and in combination with DNA-bending and U-turn formation, governs mtDNA compaction. | - |
dc.format.extent | 17 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Oxford University Press | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1093/nar/gkw1147 | - |
dc.relation.ispartof | Nucleic Acids Research, 2016, vol. 45, num. 2, p. 951-967 | - |
dc.relation.uri | https://doi.org/10.1093/nar/gkw1147 | - |
dc.rights | cc-by-nc (c) Chakraborty et al., 2016 | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc/3.0/es | - |
dc.source | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) | - |
dc.subject.classification | ADN mitocondrial | - |
dc.subject.classification | Adenina | - |
dc.subject.classification | Genomes | - |
dc.subject.other | Mitochondrial DNA | - |
dc.subject.other | Adenine | - |
dc.subject.other | Genomes | - |
dc.title | DNA structure directs positioning of the mitochondrial genome packaging protein Abf2p. | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 668748 | - |
dc.date.updated | 2017-09-29T10:34:41Z | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/291433/EU//SIMDNA | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/261460/EU//GUMS AND JOINTS | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/H2020/676556/EU//MuG | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/306029/EU//TRIGGER | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/H2020/675728/EU//BioExcel | - |
dc.relation.projectID | info:eu-repo/grantAgreement/EC/FP7/290246/EU//RAPID | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 27899643 | - |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) |
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File | Description | Size | Format | |
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668748.pdf | 9.48 MB | Adobe PDF | View/Open |
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