YeeJ is an inverse autotransporter from Escherichia coli that binds to peptidoglycan and promotes biofilm formation
Identifieur interne : 000029 ( Main/Exploration ); précédent : 000028; suivant : 000030YeeJ is an inverse autotransporter from Escherichia coli that binds to peptidoglycan and promotes biofilm formation
Auteurs : Marta Martinez-Gil [Espagne] ; Kelvin G. K. Goh ; Elze Rackaityte [États-Unis] ; Chizuko Sakamoto ; Bianca Audrain ; Danilo G. Moriel [Italie] ; Makrina Totsika ; Jean-Marc Ghigo ; Mark A. Schembri ; Christophe BeloinSource :
- Scientific Reports [ 2045-2322 ] ; 2017.
Abstract
Url:
DOI: 10.1038/s41598-017-10902-0
PubMed: 28900103
PubMed Central: 5595812
Affiliations:
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Le document en format XML
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28 rue du Dr. Roux, 75724 Paris, CEDEX 15 France</nlm:aff>
<wicri:noCountry code="subfield">CEDEX 15 France</wicri:noCountry>
</affiliation>
</author>
</analytic>
<series><title level="j">Scientific Reports</title>
<idno type="eISSN">2045-2322</idno>
<imprint><date when="2017">2017</date>
</imprint>
</series>
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<front><div type="abstract" xml:lang="en"><p id="Par1"><italic>Escherichia coli</italic>
is a commensal or pathogenic bacterium that can survive in diverse environments. Adhesion to surfaces is essential for <italic>E. coli</italic>
colonization, and thus it is important to understand the molecular mechanisms that promote this process in different niches. Autotransporter proteins are a class of cell-surface factor used by <italic>E. coli</italic>
for adherence. Here we characterized the regulation and function of YeeJ, a poorly studied but widespread representative from an emerging class of autotransporter proteins, the inverse autotransporters (IAT). We showed that the <italic>yeeJ</italic>
gene is present in ~40% of 96 completely sequenced <italic>E. coli</italic>
genomes and that YeeJ exists as two length variants, albeit with no detectable functional differences. We demonstrated that YeeJ promotes biofilm formation in different settings through exposition at the cell-surface. We also showed that YeeJ contains a LysM domain that interacts with peptidoglycan and thus assists its localization into the outer membrane. Additionally, we identified the Polynucleotide Phosphorylase PNPase as a repressor of <italic>yeeJ</italic>
transcription. Overall, our work provides new insight into YeeJ as a member of the recently defined IAT class, and contributes to our understanding of how commensal and pathogenic <italic>E. coli</italic>
colonise their environments.</p>
</div>
</front>
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</author>
<author><name sortKey="Reisner, A" uniqKey="Reisner A">A Reisner</name>
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<author><name sortKey="Klemm, P" uniqKey="Klemm P">P Klemm</name>
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</analytic>
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<biblStruct><analytic><author><name sortKey="Martinez, E" uniqKey="Martinez E">E Martinez</name>
</author>
<author><name sortKey="Bartolome, B" uniqKey="Bartolome B">B Bartolome</name>
</author>
<author><name sortKey="De La Cruz, F" uniqKey="De La Cruz F">F de la Cruz</name>
</author>
</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Lutz, R" uniqKey="Lutz R">R Lutz</name>
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<author><name sortKey="Bujard, H" uniqKey="Bujard H">H Bujard</name>
</author>
</analytic>
</biblStruct>
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</author>
<author><name sortKey="Sonntag, I" uniqKey="Sonntag I">I Sonntag</name>
</author>
<author><name sortKey="Hindennach, I" uniqKey="Hindennach I">I Hindennach</name>
</author>
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<country name="Italie"><noRegion><name sortKey="Moriel, Danilo G" sort="Moriel, Danilo G" uniqKey="Moriel D" first="Danilo G." last="Moriel">Danilo G. Moriel</name>
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