Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences.
To identify proteins that interact with HSP47, an endoplasmic reticulum (ER)-resident molecular chaperone, a yeast two-hybrid screening was performed using mouse full-length HSP47 including an N-terminal signal sequence as a bait. Analysis of several positive clones led to the identification and cloning of a novel gene, ubin, encoding a ubiquitin-like ... protein. Unlike other ubiquitin-like proteins, UBIN was shown to interact with signal sequences of various secretory and ER-luminal proteins, including HSP47, but not interact with signal sequences of mitochondrial targeting in two-hybrid system. The possible function of UBIN will be discussed with regards to novel characteristics of binding to signal sequences for ER targeting.
Mesh Terms:
3T3 Cells, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Endoplasmic Reticulum, Fluorescent Antibody Technique, Indirect, Gene Expression Profiling, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Sorting Signals, Protein Transport, RNA, Messenger, Sequence Alignment, Sequence Deletion, Tumor Cells, Cultured, Two-Hybrid System Techniques, Ubiquitins
3T3 Cells, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Endoplasmic Reticulum, Fluorescent Antibody Technique, Indirect, Gene Expression Profiling, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Protein Sorting Signals, Protein Transport, RNA, Messenger, Sequence Alignment, Sequence Deletion, Tumor Cells, Cultured, Two-Hybrid System Techniques, Ubiquitins
Biochem. Biophys. Res. Commun.
Date: Jan. 19, 2001
PubMed ID: 11162551
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