Abstract
Synaptobrevin is a tail-anchored protein with a hydrophobic C-terminal transmembrane segment that inserts into the endoplasmic reticulum membrane independently of the SRP/Sec61p pathway. Here, we show that idealized hydrophobic segments composed of 11-17 leucines and 1 valine function as insertion signals in vitro, whereas shorter segments do not. These results suggest that there are no specific requirements beyond overall hydrophobicity for C-terminal endoplasmic reticulum insertion signals.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Consensus Sequence
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DNA / chemistry
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DNA / metabolism
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Dogs
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Endoplasmic Reticulum / metabolism*
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Humans
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Membrane Proteins / biosynthesis
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism*
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Microsomes / metabolism*
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Molecular Sequence Data
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Mutagenesis, Insertional
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Mutagenesis, Site-Directed
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Nerve Tissue Proteins / biosynthesis
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism
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Pancreas / metabolism
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Peptides*
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Protein Biosynthesis
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R-SNARE Proteins
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Reticulocytes / metabolism
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Sequence Deletion
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
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Transcription, Genetic
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Transfection
Substances
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Membrane Proteins
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Nerve Tissue Proteins
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Peptides
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R-SNARE Proteins
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polyleucine
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DNA