Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/4400
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMondal, Anish Kumar-
dc.contributor.authorVerma, Paras-
dc.contributor.authorSengupta, Nayanika-
dc.contributor.authorDutta, Somnath-
dc.contributor.authorPandit, Shashi Bhushan-
dc.contributor.authorChattopadhyay, Kausik-
dc.date.accessioned2023-08-08T18:22:55Z-
dc.date.available2023-08-08T18:22:55Z-
dc.date.issued2021-
dc.identifier.citationMolecular Microbiology, 115(4), 508-525.en_US
dc.identifier.urihttps://doi.org/10.1111/mmi.14631-
dc.identifier.urihttp://hdl.handle.net/123456789/4400-
dc.descriptionOnly IISER Mohali authors are available in the record.en_US
dc.description.abstractβ-barrel pore-forming toxins perforate cell membranes by forming oligomeric β-barrel pores. The most crucial step is the membrane-insertion of the pore-forming motifs that create the transmembrane β-barrel scaffold. Molecular mechanism that regulates structural reorganization of these pore-forming motifs during β-barrel pore-formation still remains elusive. Using Vibrio cholerae cytolysin as an archetypical example of the β-barrel pore-forming toxin, we show that a key tyrosine residue (Y321) in the hinge region of the pore-forming motif plays crucial role in this process. Mutation of Y321 abrogates oligomerization of the membrane-bound toxin protomers, and blocks subsequent steps of pore-formation. Our study suggests that the presence of Y321 in the hinge region of the pore-forming motif is crucial for the toxin molecule to sense membrane-binding, and to trigger essential structural rearrangements required for the subsequent oligomerization and pore-formation process. Such a regulatory mechanism of pore-formation by V. cholerae cytolysin has not been documented earlier in the structurally related β-barrel pore-forming toxins.en_US
dc.language.isoen_USen_US
dc.publisherWileyen_US
dc.subjectTyrosineen_US
dc.subjecthinge regionen_US
dc.subjectpore-formingen_US
dc.subjectoligomeric β-barrelen_US
dc.titleTyrosine in the hinge region of the pore-forming motif regulates oligomeric β-barrel pore formation by Vibrio cholerae cytolysinen_US
dc.typeArticleen_US
Appears in Collections:Research Articles

Files in This Item:
File Description SizeFormat 
Need To Add…Full Text_PDF..pdfOnly IISER Mohali authors are available in the record.15.36 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.