Abstract：
:The human invariant chain (I gamma) of class II histocompatibility antigens spans the membrane of the endoplasmic reticulum once. It exposes a small amino-terminal domain on the cytoplasmic side and a carboxy-terminal, glycosylated domain on the exoplasmic side of the membrane. When the exoplasmic domain of I gamma is replaced by the cytoplasmic protein chloramphenicol acetyltransferase (CAT), CAT becomes the exoplasmic, glycosylated domain of the resulting membrane protein I gamma CAT. Deletion of the hydrophilic cytoplasmic domain from I gamma CAT gives rise to a secreted protein from which an amino-terminal segment is cleaved, most likely by signal peptidase. We conclude that the membrane-spanning region of I gamma contains a signal sequence in its amino-terminal half and that hydrophilic residues at the amino-terminal end of a signal sequence can determine cleavage by signal peptidase.
journal_name
Celljournal_title
Cellauthors
Lipp J,Dobberstein Bdoi
10.1016/0092-8674(86)90710-5subject
Has Abstractpub_date
1986-09-26 00:00:00pages
1103-12issue
7eissn
0092-8674issn
1097-4172pii
0092-8674(86)90710-5journal_volume
46pub_type
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