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Vol. 10, Issue 7, 2461-2474, July 1999
and
*Institut für Biochemie und Molekularbiologie and
Two major routes of preprotein targeting into mitochondria are
known. Preproteins carrying amino-terminal signals mainly use Tom20,
the general import pore (GIP) complex and the Tim23-Tim17 complex.
Preproteins with internal signals such as inner membrane carriers use
Tom70, the GIP complex, and the special Tim pathway, involving small
Tims of the intermembrane space and Tim22-Tim54 of the inner membrane.
Little is known about the biogenesis and assembly of the Tim proteins
of this carrier pathway. We report that import of the preprotein of
Tim22 requires Tom20, although it uses the carrier Tim route. In
contrast, the preprotein of Tim54 mainly uses Tom70, yet it follows the
Tim23-Tim17 pathway. The positively charged amino-terminal region of
Tim54 is required for membrane translocation but not for targeting to
Tom70. In addition, we identify two novel homologues of the small Tim
proteins and show that targeting of the small Tims follows a third new route where surface receptors are dispensable, yet Tom5 of the GIP
complex is crucial. We conclude that the biogenesis of Tim proteins of
the carrier pathway cannot be described by either one of the two major
import routes, but involves new types of import pathways composed of
various features of the hitherto known routes, including crossing over
at the level of the GIP.
Institut für Biologie, Universität
Freiburg, D-79104 Freiburg, Germany
Corresponding author. E-mail
address: pfanner{at}uni-freiburg.de.
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