FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2247646158> ?p ?o ?g. }

• W2247646158 abstract "The type II secretion system (T2SS) is widely exploited by Gram-negative bacteria to secrete diverse virulence factors from the periplasm into the extra-cellular milieu. The phytopathogenic bacterium Dickeya dadanti (ex. Erwinia chrysanthemi) uses this system, named Out, to secrete several cell-wall degrading enzymes that cause soft-rot disease of many plants. The two core components of the Out system, the inner membrane protein OutC and the secretin OutD, which forms a secretion pore in the outer membrane, are involved in secretion specificity. The interaction between OutC and OutD could assure the structural and functional integrity of the secretion system by connecting the two membranes. To understand structure-function relationships between these two components and characterize their interaction sites, we applied an integrative approach involving in vivo cysteine scanning and disulfide cross-linking analysis, truncation analysis of OutC and OutD combined with in vitro GST pull-down, and structural analysis of these proteins and of their interactions by NMR. Our results indicate the presence of at least three interacting sites between the periplasmic regions of OutC and OutD and suggest a β-strand addition mechanism for these interactions. We demonstrated that one site of the HR domain of OutC can interact with two distinct sites of OutD suggesting an alternative mode of their interactions. The presence of exoproteins or/and the inner membrane components of the system OutE-L-M differently alters the affinity of the three OutC-OutD interacting sites. We suggest that successive interactions between these distinct regions of OutC and OutD may have functional importance in switching the secretion machinery between different functional states. To study the mechanism of the targeting and assembly of the secretin OutD into the outer membrane, we exploited the interactions between OutD and two auxiliary proteins, i.e., the inner membrane protein OutB and the outer membrane lipoprotein OutS. We showed a direct interaction between the periplasmic domain of OutB and the N0 domain of OutD. Structure-function analysis of OutS-OutD complex shows that the pilotin OutS binds tightly to 18 residues close to the C-terminus of the secretin subunit causing this unstructured region to become helical on forming the complex. This work allows us to better understand the assembly and function mechanism of the type II secretion system." @default.
• W2247646158 created "2016-06-24" @default.
• W2247646158 creator A5025887687 @default.
• W2247646158 date "2012-02-10" @default.
• W2247646158 modified "2023-09-27" @default.
• W2247646158 title "Molecular characterization of the type II secretion system of the phytopathogenic bacterium Dickeya dadantii : structural and functional studies of the interaction of OutC and OutD" @default.
• W2247646158 hasPublicationYear "2012" @default.
• W2247646158 type Work @default.
• W2247646158 sameAs 2247646158 @default.
• W2247646158 citedByCount "0" @default.
• W2247646158 crossrefType "dissertation" @default.
• W2247646158 hasAuthorship W2247646158A5025887687 @default.
• W2247646158 hasConcept C104317684 @default.
• W2247646158 hasConcept C12554922 @default.
• W2247646158 hasConcept C146587185 @default.
• W2247646158 hasConcept C201663137 @default.
• W2247646158 hasConcept C2778827730 @default.
• W2247646158 hasConcept C41625074 @default.
• W2247646158 hasConcept C49039625 @default.
• W2247646158 hasConcept C547475151 @default.
• W2247646158 hasConcept C55493867 @default.
• W2247646158 hasConcept C60987743 @default.
• W2247646158 hasConcept C65871279 @default.
• W2247646158 hasConcept C86803240 @default.
• W2247646158 hasConceptScore W2247646158C104317684 @default.
• W2247646158 hasConceptScore W2247646158C12554922 @default.
• W2247646158 hasConceptScore W2247646158C146587185 @default.
• W2247646158 hasConceptScore W2247646158C201663137 @default.
• W2247646158 hasConceptScore W2247646158C2778827730 @default.
• W2247646158 hasConceptScore W2247646158C41625074 @default.
• W2247646158 hasConceptScore W2247646158C49039625 @default.
• W2247646158 hasConceptScore W2247646158C547475151 @default.
• W2247646158 hasConceptScore W2247646158C55493867 @default.
• W2247646158 hasConceptScore W2247646158C60987743 @default.
• W2247646158 hasConceptScore W2247646158C65871279 @default.
• W2247646158 hasConceptScore W2247646158C86803240 @default.
• W2247646158 hasLocation W22476461581 @default.
• W2247646158 hasOpenAccess W2247646158 @default.
• W2247646158 hasPrimaryLocation W22476461581 @default.
• W2247646158 hasRelatedWork W1953009028 @default.
• W2247646158 hasRelatedWork W1996433261 @default.
• W2247646158 hasRelatedWork W2007194419 @default.
• W2247646158 hasRelatedWork W2027181869 @default.
• W2247646158 hasRelatedWork W2038718832 @default.
• W2247646158 hasRelatedWork W2052812619 @default.
• W2247646158 hasRelatedWork W2068746418 @default.
• W2247646158 hasRelatedWork W2091836230 @default.
• W2247646158 hasRelatedWork W2105229000 @default.
• W2247646158 hasRelatedWork W2112558684 @default.
• W2247646158 hasRelatedWork W2138742566 @default.
• W2247646158 hasRelatedWork W2765481851 @default.
• W2247646158 hasRelatedWork W2767072678 @default.
• W2247646158 hasRelatedWork W2797446131 @default.
• W2247646158 hasRelatedWork W2806695756 @default.
• W2247646158 hasRelatedWork W2899958772 @default.
• W2247646158 hasRelatedWork W2911831690 @default.
• W2247646158 hasRelatedWork W3118785262 @default.
• W2247646158 hasRelatedWork W3184320097 @default.
• W2247646158 hasRelatedWork W3188255407 @default.
• W2247646158 isParatext "false" @default.
• W2247646158 isRetracted "false" @default.
• W2247646158 magId "2247646158" @default.
• W2247646158 workType "dissertation" @default.