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Sökning: id:"swepub:oai:DiVA.org:umu-146348" > Heterologous comple...

Heterologous complementation studies with the YscX and YscY protein families reveals a specificity for Yersinia pseudotuberculosis type III secretion

Gurung, Jyoti M. (författare)
Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Umeå Centre for Microbial Research (UCMR),Francis
Amer, Ayad (författare)
Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Umeå Centre for Microbial Research (UCMR),Francis
Francis, Monika (författare)
Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Umeå Centre for Microbial Research (UCMR),Francis
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Costa, Tiago (författare)
Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Umeå Centre for Microbial Research (UCMR),Francis
Chen, Shiyun (författare)
Zavialov, Anton V. (författare)
Francis, Matthew S. (författare)
Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Umeå Centre for Microbial Research (UCMR),Francis
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 (creator_code:org_t)
2018-03-16
2018
Engelska.
Ingår i: Frontiers in Cellular and Infection Microbiology. - : Frontiers Research Foundation. - 2235-2988. ; 8
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Mikrobiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Microbiology (hsv//eng)

Nyckelord

T3S chaperone
secretion hierarchy
substrate sorting
LcrH/SycD
YscV
protein-protein interaction
mikrobiologi
Microbiology
molekylärbiologi
Molecular Biology
Infectious Diseases
infektionssjukdomar

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