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A eukaryotic carboxyl‐terminal signal sequence translocating large hydrophilic domains across membranes
Author(s) -
Zhong Xiaotian,
Malhotra Rajeev,
Guidotti Guido
Publication year - 2005
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/j.febslet.2005.09.036
Subject(s) - signal peptide , membrane , transmembrane domain , sequence (biology) , transmembrane protein , n terminus , c terminus , peptide sequence , golgi apparatus , protein sorting signals , biochemistry , biology , extracellular , membrane protein , microbiology and biotechnology , biophysics , amino acid , endoplasmic reticulum , receptor , gene
Yeast Golgi ecto‐ATPase Ynd1p is an unusual type III membrane protein with the longest translocated N‐terminus reported. Sequential deletion analysis reveals that translocation of this 500‐residue‐long hydrophilic domain across the membranes requires the C‐terminal transmembrane domain of Ynd1p and its flanking regions. Additional studies indicate that the topogenic sequence of Ynd1p overrides the effect of a reverse signal‐anchor sequence present at the N‐terminus of Ynd1p, while it is not affected by a classic signal sequence at the N‐terminus. When placed at the C‐terminal end, the sequence can translocate large extracellular domains of two membrane proteins across the membranes. The data demonstrate the existence of a true eukaryotic C‐terminal signal sequence.