Obsah souboru
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<JournalTitle>Journal of Applied Biomedicine</JournalTitle>
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<CoverDate Year="2010" Month="9" Day="1"/>
<CoverDisplay>Number 3 / September 2010</CoverDisplay>
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<ArticleDOI>10.2478/v10136-009-0018-4</ArticleDOI>
<ArticlePII>M47K455473872925</ArticlePII>
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<ArticleTitle Language="En">Voyage of RepA protein from plasmid DNA replication through amyloid aggregation towards synthetic biology</ArticleTitle>
<ArticleFirstPage>151</ArticleFirstPage>
<ArticleLastPage>158</ArticleLastPage>
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<RegistrationDate>20100708</RegistrationDate>
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<ArticleHeader>
<AuthorGroup>
<Author AffiliationID="A1">
<GivenName>Rafael</GivenName>
<Initials/>
<FamilyName>Giraldo</FamilyName>
<Degrees/>
<Roles/>
</Author>
<Author AffiliationID="A1">
<GivenName>María</GivenName>
<Initials>Elena</Initials>
<FamilyName>Fernández-Tresguerres</FamilyName>
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<Roles/>
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<OrgName>Department of Chemical and Physical Biology, Centro de Investigaciones Biológicas (CIB) - CSIC, Madrid, Spain</OrgName>
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<Abstract Language="En">DNA replication of plasmids in Gram-negative bacteria has been an object of study at CIB-CSIC for nearly 30 years. We have been focused on the enterobacterial antibiotic resistance factor R1 (1981-1992) and the pPS10 replicon from the phytopathogen <i>Pseudomonas savastanoi</i> (since 1984). Our group has used multidisciplinary (genetic, biochemical and biophysical-structural) approaches to unravel the molecular mechanism for the activation of RepA. Rep-type plasmidic proteins are either transcriptional repressors or replication initiators/inhibitors, depending on their association state (dimers vs. monomers) and targeting of alternative (operator or iteron) DNA sites. We discovered that allosteric DNA-binding remodels the structure of RepA N-terminal domain (WH1), transforming α-helical portions into β-strands. This precisely tunes the distances between the DNA reading heads in WH1 and the C-terminal domain (WH2), to match the target operator or iteron sequences. We have recently moved into engineering such structural transformation in RepA-WH1 to build-up synthetic protein devices that allow for customized ligand (DNA)-promoted amyloidogenesis. Our basic studies on plasmid DNA replication are relevant for settling the bases of a minimalist bacterial model to tackle transmissible amyloid proteinopathies and are a valuable tool for bottom-up synthetic biology.</Abstract>
<KeywordGroup Language="En">
<Keyword>plasmid replication</Keyword>
</KeywordGroup>
<KeywordGroup Language="En">
<Keyword>protein amyloids</Keyword>
</KeywordGroup>
<KeywordGroup Language="En">
<Keyword>protein-DNA interactions</Keyword>
</KeywordGroup>
<KeywordGroup Language="En">
<Keyword>RepA protein</Keyword>
</KeywordGroup>
<KeywordGroup Language="En">
<Keyword>synthetic biology</Keyword>
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<biblist>
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</bib-other>
<bib-other>
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</bib-other>
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