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J. Biol. Chem., Vol. 277, Issue 8, 5715-5718, February 22, 2002
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§,
,
From the The integration of the polytopic membrane protein
YidC into the inner membrane of Escherichia coli was
analyzed employing an in vitro system. Upon integration of
in vitro synthesized YidC, a 42-kDa membrane protected
fragment was detected, which could be immunoprecipitated with
polyclonal anti-YidC antibodies. The occurrence of this fragment is in
agreement with the predicted topology of YidC and probably encompasses
the first two transmembrane domains and the connecting 320-amino
acid-long periplasmic loop. The integration of YidC was strictly
dependent on the signal recognition particle and SecA. YidC
could not be integrated in the absence of SecY, SecE, or SecG,
suggesting that YidC, in contrast to its mitochondrial orthologue
Oxa1p, cannot engage a SecYEG-independent protein-conducting channel.
Institute for Biochemistry and Molecular
Biology, University Freiburg, Hermann-Herder-Stra
e 7, D-79104
Freiburg, Germany and the ¶ Institute for Biotechnology,
Forschungszentrum Jülich, D-52425 Jülich, Germany
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