TY - JOUR
T1 - Sticholysin I–II oligomerization in the absence of membranes
AU - García-Linares, Sara
AU - Amigot-Sánchez, Rafael
AU - García-Montoya, Carmen
AU - Heras-Márquez, Diego
AU - Alfonso, Carlos
AU - Luque-Ortega, Juan Román
AU - Gavilanes, José G.
AU - Martínez-del-Pozo, Álvaro
AU - Palacios-Ortega, Juan
N1 - Funding Information:
This research was supported by the Juselius Foundation (JP‐O), UCM‐Banco Santander Grants PR75/18‐21561 and PR87/19‐22556, and UnaEuropa (Unano) SF2106 (to AM‐d‐P) and Spanish Ministry of Science and Innovation PID2019‐104544GB‐I00 (CA). JP‐O has a funded doctoral student position from ISB/ÅA. JRL‐O acknowledges support from the Molecular Interactions Facility funds at the CIB‐CSIC.
Funding Information:
This research was supported by the Juselius Foundation (JP-O), UCM-Banco Santander Grants PR75/18-21561 and PR87/19-22556, and UnaEuropa (Unano) SF2106 (to AM-d-P) and Spanish Ministry of Science and Innovation PID2019-104544GB-I00 (CA). JP-O has a funded doctoral student position from ISB/?A. JRL-O acknowledges support from the Molecular Interactions Facility funds at the CIB-CSIC.
Publisher Copyright:
© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
PY - 2022/4
Y1 - 2022/4
N2 - Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.
AB - Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.
KW - actinoporins
KW - analytical ultracentrifugation
KW - pore-forming proteins
KW - sedimentation velocity
UR - http://www.scopus.com/inward/record.url?scp=85126036594&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.14326
DO - 10.1002/1873-3468.14326
M3 - Article
C2 - 35253212
AN - SCOPUS:85126036594
SN - 0014-5793
VL - 596
SP - 1029
EP - 1036
JO - FEBS Letters
JF - FEBS Letters
IS - 8
ER -