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Swapping of the N‐terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti‐aging features to the cell
Author(s) -
Reina Simona,
Palermo Vanessa,
Guarnera Andrea,
Guarino Francesca,
Messina Angela,
Mazzoni Cristina,
De Pinto Vito
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.066
Subject(s) - vdac1 , voltage dependent anion channel , porin , biochemistry , microbiology and biotechnology , mitochondrion , chemistry , hsp70 , gene isoform , biology , bacterial outer membrane , heat shock protein , gene , escherichia coli
Voltage‐dependent anion‐selective channels (VDACs) are pore‐forming proteins allowing the permeability of the mitochondrial outer membrane. The VDAC3 isoform is the least abundant and least active in a complementation assay performed in a yeast strain devoid of porin‐1. We swapped the VDAC3 N‐terminal 20 amino acids with homologous sequences from the other isoforms. The substitution of the VDAC3 N‐terminus with the VDAC1 N‐terminus caused the chimaera to become more active than VDAC1. The VDAC2 N‐terminus improved VDAC3 activity, though to a lesser extent. The VDAC3 carrying the VDAC1 N‐terminus was able to complement the lack of the yeast porin in mitochondrial respiration and in modulation of reactive oxygen species (ROS). This chimaera increased life span, indicating a more efficient bioenergetic metabolism and/or a better protection from ROS.