Search: onr:"swepub:oai:DiVA.org:umu-152249" >
14-3-3 proteins act...
14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface
-
Karlberg, Tobias (author)
-
Hornyak, Peter (author)
-
Pinto, Ana Filipa (author)
-
show more...
-
- Milanova, Stefina (author)
- Karolinska Institutet
-
Ebrahimi, Mahsa (author)
-
- Lindberg, Mikael J. (author)
- Umeå universitet,Kemiska institutionen
-
Püllen, Nikolai (author)
-
Nordström, Axel (author)
-
Löverli, Elinor (author)
-
- Caraballo, Remi (author)
- Umeå universitet,Kemiska institutionen
-
Wong, Emily V. (author)
-
Näreoja, Katja (author)
-
Thorsell, Ann-Gerd (author)
-
- Elofsson, Mikael (author)
- Umeå universitet,Kemiska institutionen
-
De la Cruz, Enrique M. (author)
-
- Björkegren, Camilla (author)
- Karolinska Institutet
-
- Schüler, Herwig (author)
- Karolinska Institutet
-
show less...
-
(creator_code:org_t)
- 2018-09-17
- 2018
- English.
-
In: Nature Communications. - : Nature Publishing Group. - 2041-1723. ; 9
- Related links:
-
https://doi.org/10.1...
-
show more...
-
https://umu.diva-por... (primary) (Raw object)
-
https://www.nature.c...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
http://kipublication...
-
show less...
Abstract
Subject headings
Close
- Pseudomonas are a common cause of hospital-acquired infections that may be lethal. ADP-ribosyltransferase activities of Pseudomonas exotoxin-S and -T depend on 14-3-3 proteins inside the host cell. By binding in the 14-3-3 phosphopeptide binding groove, an amphipathic C-terminal helix of ExoS and ExoT has been thought to be crucial for their activation. However, crystal structures of the 14-3-3 beta: ExoS and -ExoT complexes presented here reveal an extensive hydrophobic interface that is sufficient for complex formation and toxin activation. We show that C-terminally truncated ExoS ADP-ribosyltransferase domain lacking the amphipathic binding motif is active when co-expressed with 14-3-3. Moreover, swapping the amphipathic C-terminus with a fragment from Vibrio Vis toxin creates a 14-3-3 independent toxin that ADP-ribosylates known ExoS targets. Finally, we show that 14-3-3 stabilizes ExoS against thermal aggregation. Together, this indicates that 14-3-3 proteins activate exotoxin ADP-ribosyltransferase domains by chaperoning their hydrophobic surfaces independently of the amphipathic C-terminal segment.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Karlberg, Tobias
-
Hornyak, Peter
-
Pinto, Ana Filip ...
-
Milanova, Stefin ...
-
Ebrahimi, Mahsa
-
Lindberg, Mikael ...
-
show more...
-
Püllen, Nikolai
-
Nordström, Axel
-
Löverli, Elinor
-
Caraballo, Remi
-
Wong, Emily V.
-
Näreoja, Katja
-
Thorsell, Ann-Ge ...
-
Elofsson, Mikael
-
De la Cruz, Enri ...
-
Björkegren, Cami ...
-
Schüler, Herwig
-
show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
-
MEDICAL AND HEAL ...
-
and Basic Medicine
-
and Cell and Molecul ...
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Biological Scien ...
-
and Biochemistry and ...
- Articles in the publication
-
Nature Communica ...
- By the university
-
Umeå University
-
Karolinska Institutet