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Membrane translocation and insertion of NH 2 ‐terminally anchored γ‐glutamyl transpeptidase require a signal recognition particle
Author(s) -
Tate Suresh S.,
Nash Barbara
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81423-0
Subject(s) - signal recognition particle , signal peptide , chromosomal translocation , cytoplasm , enzyme , biochemistry , membrane , chemistry , sequence (biology) , n terminus , brush border , side chain , protein precursor , peptide sequence , protein targeting , biophysics , membrane protein , microbiology and biotechnology , biology , vesicle , gene , organic chemistry , polymer
The two subunits of the renal brush border enzyme, γ‐glutamyl transpeptidase (EC 2.3.2.2), are derived from a single‐chain propeptide. The membrane‐spanning domain consists of a hydrophobic sequence near its NH 2 ‐terminus and the protein is oriented with its NH 2 ‐terminus on the cytoplasmic side. The enzyme is synthesized without a cleavable signal sequence. Translocation and insertion of this enzyme have been shown to be dependent on the signal recognition particle and presumably require the same translocation machinery that other secretory and membrane proteins use for these processes.