Signal-sequence trap in mammalian and yeast cells
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Signal-sequence trap in mammalian and yeast cells : a comparison. / Galliciotti, G; Schneider, H; Wyder, L; Vitaliti, A; Wittmer, M; Ajmo, M; Klemenz, R.
in: J MEMBRANE BIOL, Jahrgang 183, Nr. 3, 01.10.2001, S. 175-82.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Signal-sequence trap in mammalian and yeast cells
T2 - a comparison
AU - Galliciotti, G
AU - Schneider, H
AU - Wyder, L
AU - Vitaliti, A
AU - Wittmer, M
AU - Ajmo, M
AU - Klemenz, R
PY - 2001/10/1
Y1 - 2001/10/1
N2 - Membrane associated and secreted proteins are translated as precursors containing a signal peptide that allows protein-insertion into the membrane of the endoplasmic reticulum and is co-translationally removed in the lumen. The ability of the signal peptide to direct a polypeptide into the secretory pathway is exploited in methods developed to select cDNAs encoding such proteins. Different strategies are known in which cDNA libraries can be screened for signal peptides by the ability of the latter to rescue the translocation of signal sequence-less proteins. In one method, a cDNA library is tested for interleukin 2 receptor alpha chain translocation to the membrane in COS cells, in another one for invertase secretion from yeast. In this work, we compared the two systems by testing six mouse signal peptides in COS and yeast cells. All of them were functional in the mammalian system, whereas only three of them in yeast. Two other sequences needed the 5' cDNA sequence flanking the ATG codon to be removed in order to enable protein translocation. Although the structure of signal sequences and the functioning of the secretory machinery are well conserved from prokaryotes to eukaryotes, it seems evident that not all signal peptides can be interchanged between different proteins and organisms. In particular, signal peptides that are functional in the mammalian system do not necessarily lead to protein translocation in yeast.
AB - Membrane associated and secreted proteins are translated as precursors containing a signal peptide that allows protein-insertion into the membrane of the endoplasmic reticulum and is co-translationally removed in the lumen. The ability of the signal peptide to direct a polypeptide into the secretory pathway is exploited in methods developed to select cDNAs encoding such proteins. Different strategies are known in which cDNA libraries can be screened for signal peptides by the ability of the latter to rescue the translocation of signal sequence-less proteins. In one method, a cDNA library is tested for interleukin 2 receptor alpha chain translocation to the membrane in COS cells, in another one for invertase secretion from yeast. In this work, we compared the two systems by testing six mouse signal peptides in COS and yeast cells. All of them were functional in the mammalian system, whereas only three of them in yeast. Two other sequences needed the 5' cDNA sequence flanking the ATG codon to be removed in order to enable protein translocation. Although the structure of signal sequences and the functioning of the secretory machinery are well conserved from prokaryotes to eukaryotes, it seems evident that not all signal peptides can be interchanged between different proteins and organisms. In particular, signal peptides that are functional in the mammalian system do not necessarily lead to protein translocation in yeast.
KW - Animals
KW - Base Sequence
KW - COS Cells
KW - Endothelium, Vascular
KW - Eukaryotic Cells
KW - Gene Library
KW - Glycoside Hydrolases
KW - Mammals
KW - Membrane Proteins
KW - Mice
KW - Molecular Sequence Data
KW - Peptides
KW - Protein Sorting Signals
KW - Protein Transport
KW - Receptors, Interleukin-2
KW - Species Specificity
KW - Yeasts
KW - beta-Fructofuranosidase
M3 - SCORING: Journal article
C2 - 11696859
VL - 183
SP - 175
EP - 182
JO - J MEMBRANE BIOL
JF - J MEMBRANE BIOL
SN - 0022-2631
IS - 3
ER -