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2012-12-21Zeitschriftenartikel DOI: 10.1128/JB.02171-12
Protein-Protein Interaction Domains of Bacillus subtilis DivIVA
dc.contributor.authorBaarle, Suey van
dc.contributor.authorCelik, Ilkay Nazli
dc.contributor.authorKaval, Karan Gautam
dc.contributor.authorBramkamp, Marc
dc.contributor.authorHamoen, Leendert W.
dc.contributor.authorHalbedel, Sven
dc.date.accessioned2018-05-07T16:50:11Z
dc.date.available2018-05-07T16:50:11Z
dc.date.created2013-07-22
dc.date.issued2012-12-21none
dc.identifier.otherhttp://edoc.rki.de/oa/articles/rei2GyLt3Y6xw/PDF/20C61mEUo5C1A.pdf
dc.identifier.urihttp://edoc.rki.de/176904/1604
dc.description.abstractDivIVA proteins are curvature-sensitive membrane binding proteins that recruit other proteins to the poles and the division septum. They consist of a conserved N-terminal lipid binding domain fused to a less conserved C-terminal domain. DivIVA homologues interact with different proteins involved in cell division, chromosome segregation, genetic competence, or cell wall synthesis. It is unknown how DivIVA interacts with these proteins, and we used the interaction of Bacillus subtilis DivIVA with MinJ and RacA to investigate this. MinJ is a transmembrane protein controlling division site selection, and the DNA-binding protein RacA is crucial for chromosome segregation during sporulation. Initial bacterial two-hybrid experiments revealed that the C terminus of DivIVA appears to be important for recruiting both proteins. However, the interpretation of these results is limited since it appeared that C-terminal truncations also interfere with DivIVA oligomerization. Therefore, a chimera approach was followed, making use of the fact that Listeria monocytogenes DivIVA shows normal polar localization but is not biologically active when expressed in B. subtilis. Complementation experiments with different chimeras of B. subtilis and L. monocytogenes DivIVA suggest that MinJ and RacA bind to separate DivIVA domains. Fluorescence microscopy of green fluorescent protein-tagged RacA and MinJ corroborated this conclusion and suggests that MinJ recruitment operates via the N-terminal lipid binding domain, whereas RacA interacts with the C-terminal domain. We speculate that this difference is related to the cellular compartments in which MinJ and RacA are active: the cell membrane and the cytoplasm, respectively.eng
dc.language.isoeng
dc.publisherRobert Koch-Institut, Infektionskrankheiten / Erreger
dc.subjectAmino Acid Sequenceeng
dc.subjectSequence Alignmenteng
dc.subjectBacillus subtilis/chemistryeng
dc.subjectBacillus subtilis/geneticseng
dc.subjectBacillus subtilis/metabolismeng
dc.subjectBacterial Proteins/chemistryeng
dc.subjectBacterial Proteins/metabolismeng
dc.subjectCell Cycle Proteins/chemistryeng
dc.subjectCell Cycle Proteins/metabolismeng
dc.subjectCell Divisioneng
dc.subjectCell Wall/metabolismeng
dc.subjectChromosome Segregationeng
dc.subjectCrystallography X-Rayeng
dc.subjectDNA-Binding Proteins/geneticseng
dc.subjectDNA-Binding Proteins/metabolismeng
dc.subjectGreen Fluorescent Proteins/geneticseng
dc.subjectListeria monocytogenes/chemistryeng
dc.subjectListeria monocytogenes/geneticseng
dc.subjectMembrane Proteins/geneticseng
dc.subjectMembrane Proteins/metabolismeng
dc.subjectProtein Interaction Domains and Motifseng
dc.subjectRecombinant Fusion Proteins/chemistryeng
dc.subject.ddc610 Medizin
dc.titleProtein-Protein Interaction Domains of Bacillus subtilis DivIVA
dc.typeperiodicalPart
dc.identifier.urnurn:nbn:de:0257-10032002
dc.identifier.doi10.1128/JB.02171-12
dc.identifier.doihttp://dx.doi.org/10.25646/1529
local.edoc.container-titleJournal of Bacteriology
local.edoc.container-textvan Baarle, S., Celik, I.N., Kaval, K.G., Bramkamp, M., Hamoen, L.W., Halbedel, S. Protein-protein interaction domains of Bacillus subtilis DivIVA (2013) Journal of Bacteriology, 195 (5), pp. 1012-1021.
local.edoc.fp-subtypeArtikel
local.edoc.type-nameZeitschriftenartikel
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-urlhttp://jb.asm.org/content/195/5/1012
local.edoc.container-publisher-nameAmerican Society for Microbiology
local.edoc.container-volume195
local.edoc.container-issue5
local.edoc.container-year2013

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