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Vol. 11, Issue 1, 103-116, January 2000
Department of Cell Biology and Anatomy, The Johns Hopkins School of
Medicine, Baltimore, Maryland 21205
The mitochondrial inner membrane contains two separate translocons:
one required for the translocation of matrix-targeted proteins (the
Tim23p-Tim17p complex) and one for the insertion of polytopic proteins
into the mitochondrial inner membrane (the Tim54p-Tim22p complex). To
identify new members of the Tim54p-Tim22p complex, we screened for
high-copy suppressors of the temperature-sensitive tim54-1 mutant. We identified a new gene,
TIM18, that encodes an integral protein of the inner
membrane. The following genetic and biochemical observations suggest
that the Tim18 protein is part of the Tim54p-Tim22p complex in the
inner membrane: multiple copies of TIM18 suppress the
tim54-1 growth defect; the
tim18::HIS3 disruption is synthetically lethal
with tim54-1; Tim54p and Tim22p can be coimmune
precipitated with the Tim18 protein; and Tim18p, along with Tim54p and
Tim22p, is detected in an ~300-kDa complex after blue native
electrophoresis. We propose that Tim18p is a new component of the
Tim54p-Tim22p machinery that facilitates insertion of polytopic
proteins into the mitochondrial inner membrane.
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