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Vol. 10, Issue 10, 3289-3299, October 1999
Biozentrum der Universität Basel, CH-4055 Basel, Switzerland
To identify yeast cytosolic proteins that mediate targeting of
precursor proteins to mitochondria, we developed an in vitro import
system consisting of purified yeast mitochondria and a radiolabeled
mitochondrial precursor protein whose C terminus was still attached to
the ribosome. In this system, the N terminus of the nascent chain was
translocated across both mitochondrial membranes, generating a
translocation intermediate spanning both membranes. The nascent chain
could then be completely chased into the mitochondrial matrix after
release from the ribosome. Generation of this import intermediate was
dependent on a mitochondrial membrane potential, mitochondrial surface
proteins, and was stimulated by proteins that could be released from
the ribosomes by high salt. The major salt-released stimulatory factor
was yeast nascent polypeptide-associated complex (NAC). Purified NAC
fully restored import of salt-washed ribosome-bound nascent chains by
enhancing productive binding of the chains to mitochondria. We propose
that ribosome-associated NAC facilitates recognition of nascent
precursor chains by the mitochondrial import machinery.
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