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VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways
Author(s) -
Müller Anne,
Rassow Joachim,
Grimm Jan,
Machuy Nikolaus,
Meyer Thomas F.,
Rudel Thomas
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.8.1916
Subject(s) - neisseria gonorrhoeae , biology , porin , voltage dependent anion channel , microbiology and biotechnology , neisseria , bacterial outer membrane , genetics , bacteria , escherichia coli , gene
The human pathogen Neisseria gonorrhoeae induces host cell apoptosis during infection by delivering the outer membrane protein PorB to the host cell's mitochondria. PorB is a pore‐forming β‐barrel protein sharing several features with the mitochondrial voltage‐dependent anion channel (VDAC), which is involved in the regulation of apoptosis. Here we show that PorB of pathogenic Neisseria species produced by host cells is efficiently targeted to mitochondria. Imported PorB resides in the mitochondrial outer membrane and forms multimers with similar sizes as in the outer bacterial membrane. The mitochondria completely lose their membrane potential, a characteristic previously observed in cells infected with gonococci or treated with purified PorB. Closely related bacterial porins of non‐pathogenic Neisseria mucosa or Escherichia coli remain in the cytosol. Import of PorB into mitochondria in vivo is independent of a linear signal sequence. Insertion of PorB into the mitochondrial outer membrane in vitro depends on the activity of Tom5, Tom20 and Tom40, but is independent of Tom70. Our data show that human VDAC and bacterial PorB are imported into mitochondria by a similar mechanism.