umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Francis)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Francis)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Francis)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Francis)
Show others and affiliations
2018 (English)In: Frontiers in Cellular and Infection Microbiology, E-ISSN 2235-2988, Vol. 8, article id 80Article in journal (Refereed) Published
Abstract [en]

Type III secretion systems harbored by several Gram-negative bacteria are often used to deliver host-modulating effectors into infected eukaryotic cells. About 20 core proteins are needed for assembly of a secretion apparatus. Several of these proteins are genetically and functionally conserved in type III secretion systems of bacteria associated with invertebrate or vertebrate hosts. In the Ysc family of type III secretion systems are two poorly characterized protein families, the YscX family and the YscY family. In the plasmid-encoded Ysc-Yop type III secretion system of human pathogenic Yersinia species, YscX is a secreted substrate while YscY is its non-secreted cognate chaperone. Critically, neither an yscX nor yscY null mutant of Yersinia is capable of type III secretion. In this study, we show that the genetic equivalents of these proteins produced as components of other type III secretion systems of Pseudomonas aeruginosa (PscX and PscY), Aeromonas species (AscX and AscY), Vibrio species (VscX and VscY), and Photorhabdus luminescens (SctX and SctY) all possess an ability to interact with its native cognate partner and also establish cross-reciprocal binding to non-cognate partners as judged by a yeast two-hybrid assay. Moreover, a yeast three-hybrid assay also revealed that these heterodimeric complexes could maintain an interaction with YscV family members, a core membrane component of all type III secretion systems. Despite maintaining these molecular interactions, only expression of the native yscX in the near full-length yscX deletion and native yscY in the near full-length yscY deletion were able to complement for their general substrate secretion defects. Hence, YscX and YscY must have co-evolved to confer an important function specifically critical for Yersinia type III secretion.

Place, publisher, year, edition, pages
Frontiers Research Foundation , 2018. Vol. 8, article id 80
Keywords [en]
T3S chaperone, secretion hierarchy, substrate sorting, LcrH/SycD, YscV, protein-protein interaction
National Category
Microbiology
Research subject
Microbiology; Molecular Biology; Infectious Diseases
Identifiers
URN: urn:nbn:se:umu:diva-146348DOI: 10.3389/fcimb.2018.00080ISI: 000427608900001PubMedID: 29616194OAI: oai:DiVA.org:umu-146348DiVA, id: diva2:1195588
Funder
Swedish Research CouncilAvailable from: 2018-04-05 Created: 2018-04-05 Last updated: 2018-06-09Bibliographically approved

Open Access in DiVA

fulltext(10167 kB)93 downloads
File information
File name FULLTEXT01.pdfFile size 10167 kBChecksum SHA-512
32dadbdf6d6679e198d1bae320abe0c59f2d7220ad511131096a5e4bf85f687ffc838b818ced63846371304e63ab536e01aa619a52603985312eafebce2cb7b2
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Gurung, Jyoti M.Amer, AyadFrancis, MonikaCosta, TiagoFrancis, Matthew S.

Search in DiVA

By author/editor
Gurung, Jyoti M.Amer, AyadFrancis, MonikaCosta, TiagoFrancis, Matthew S.
By organisation
Department of Molecular Biology (Faculty of Science and Technology)Umeå Centre for Microbial Research (UCMR)
In the same journal
Frontiers in Cellular and Infection Microbiology
Microbiology

Search outside of DiVA

GoogleGoogle Scholar
Total: 93 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 258 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf