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J Biol Chem, Vol. 274, Issue 19, 13223-13228, May 7, 1999
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From the Bacterial periplasmic nickel-containing
hydrogenases are composed of a small subunit containing a twin-arginine
signal sequence and a large subunit devoid of an export signal. To
understand how the large subunit is translocated into the periplasm, we
cloned the hyb operon encoding the hydrogenase 2 of
Escherichia coli, constructed a deletion mutant, and
studied the mechanism of translocation of hydrogenase 2. The small
subunit (HybO) or the large subunit (HybC) accumulated in the cytoplasm
as a precursor when either of them was expressed in the absence of the
other subunit. Therefore, contrary to most classical secretory
proteins, the signal sequence of the small subunit itself is not
sufficient for membrane targeting and translocation if the large
subunit is missing. On the other hand, the small subunit was required
not only for membrane targeting of the large subunit, but also for the
acquisition of nickel by the large subunit. Most interestingly, the
signal sequence of the small subunit determines whether the large
subunit follows the Sec or the twin-arginine translocation pathway.
Taken together, these results provide for the first time compelling
evidence for a naturally occurring hitchhiker co-translocation
mechanism in bacteria.
Laboratoire de Chimie Bactérienne,
UPR9043 CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France and the
§ Institut für Biochemie und Molekularbiologie and
¶ Fakulatät für Biologie, Universität Freiburg,
Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany
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