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J Biol Chem, Vol. 273, Issue 52, 34868-34874, December 25, 1998
From the Department of Biological Sciences, University of Warwick,
Coventry CV4 7AL, United Kingdom
A subset of lumen proteins is transported across
the thylakoid membrane by a Sec-independent translocase that recognizes
a twin-arginine motif in the targeting signal. A related system operates in bacteria, apparently for the export of redox
cofactor-containing proteins. In this report we describe a key feature
of this system, the ability to transport folded proteins. The
thylakoidal system is able to transport dihydrofolate reductase (DHFR)
when an appropriate signal is attached, and the transport efficiency is
almost undiminished by the binding of folate analogs such as
methotrexate that cause the protein to fold very tightly. The system is
moreover able to transport DHFR into the lumen with methotrexate bound
in the active site, demonstrating that the 
pH-driven transport of
large, native structures is possible by this pathway. However, correct folding is not a prerequisite for transport. Truncated, malfolded DHFR
can be translocated by this system, as can physiological substrates
that are severely malfolded by the incorporation of amino acid analogs.
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