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J Biol Chem, Vol. 273, Issue 47, 30903-30908, November 20, 1998
From the Laboratoire de Génétique Moléculaire et
Cellulaire, INRA, CNRS, Institut National Agronomique
Paris-Grignon, 78850 Thiverval-Grignon, France and the
§ Georg-August Universitaet Goettingen, Zentrum
Biochemie und Molekular Zellbiologie,
37073 Goettingen, Germany
The yeast Yarrowia lipolytica is a
model organism for in vivo study of the signal recognition
particle-dependent targeting pathway. In this report, we
defined solubilization conditions and set up a fractionation procedure
of Y. lipolytica microsomes to determine the amounts of
Sec61p-containing translocation pores linked to ribosomes. In contrast
to Saccharomyces cerevisiae, from 70 to 80% of Sec61p
associates with ribosomes in this yeast. The chaperone protein Kar2p
and the Sls1p product, a resident protein of the endoplasmic reticulum
lumen, partially fractionate with this Sec61p population. Moreover,
Sls1p can be co-immunoprecipitated with Kar2p, and the two polypeptides
are shown to directly interact in the yeast two-hybrid system. A
site-directed mutagenesis was performed on the SLS1 coding
sequence that allowed us to define a functional domain in Sls1p.
Indeed, co-translational translocation of a reporter protein is
affected when one of these mutant proteins is expressed. Moreover, this
protein has lost its capacity to interact with Kar2p, and the two
lumenal polypeptides might thus cooperate to promote secretory protein
co-translational translocation.
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