Abstract
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.
Copyright 2001 Academic Press.
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Autophagy-Related Proteins
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism*
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Endoplasmic Reticulum / metabolism*
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Fluorescent Antibody Technique, Indirect
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Gene Expression Profiling
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Nuclear Proteins*
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Protein Binding
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Protein Sorting Signals / genetics
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Protein Sorting Signals / physiology*
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Protein Transport
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Sequence Alignment
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Sequence Deletion / genetics
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Tumor Cells, Cultured
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Two-Hybrid System Techniques
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Ubiquitins / chemistry
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Ubiquitins / genetics*
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Ubiquitins / metabolism*
Substances
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Autophagy-Related Proteins
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Carrier Proteins
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Nuclear Proteins
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Protein Sorting Signals
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RNA, Messenger
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UBIN protein, mouse
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UBQLN4 protein, human
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Ubiquitins