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(Received for publication, May 10, 1996, and in revised form, August 30, 1996)
From the Istituto Nazionale della Nutrizione, Via Ardeatina 546, 00178 Roma, Italy, the ¶ Dipartimento di Medicina Sperimentale e
Patologia, Università "La Sapienza," Roma, Italy, and the
** Department of Cell Biology, New York University Medical Center,
New York, New York 10016-6402
A search for novel genes that are up-regulated
during development and differentiation of the epithelial cells of the
intestinal mucosa led us to the isolation of the Dri 42 cDNA clone (Dri, differentially expressed in rat intestine). The
nucleotide sequence of the full-length cDNA has shown that it
encodes a 35.5-kDa protein with one consensus sequence for
N-linked glycosylation and alternating hydrophilic and
hydrophobic domains. To determine the intracellular localization of Dri
42 we have raised polyclonal antibodies in hens against a bacterially
produced Dri 42-glutathione S-transferase fusion protein.
Immunofluorescence detection with these antibodies has shown specific
staining of the endoplasmic reticulum (ER) in the relatively
undifferentiated fetal rat intestinal cell line FRIC B and in sections
of rat small intestine. ER membrane localization of Dri 42 was
confirmed by laser confocal microscopy of polarized Madin-Darby canine
kidney cells overexpressing a Dri 42-chloramphenicol acetyltransferase
(CAT) fusion protein by transfection. Pulse labeling experiments on
transiently transfected cells demonstrated that the protein does not
acquire Golgi modifications up to 4 h after synthesis, thus
indicating that Dri 42 is an ER resident protein. The transmembrane
disposition of Dri 42 was studied using in vitro insertion
of Dri 42-CAT fusion proteins into microsomal membranes. The fusion
proteins consisted of several different lengths of truncated Dri 42 and
a reporter protein, CAT, that was linked in-frame after each
hydrophobic segment. We found that hydrophobic segments H1, H3, and H5
had a signal/anchor function, and that membrane insertion of Dri 42 was
achieved co-translationally by the action of a series of alternating
insertion signals and halt transfer signals, resulting in the exposure
of both termini of the protein to the cytosolic side. The functional
implications of the structure and localization of Dri 42, whose primary
sequence does not share significant homology to any previously
described protein, are discussed.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29928-29936
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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