Abstract
The nucleotide sequence of the Saccharomyces cerevisiae gene encoding a small heat-shock protein (Hsp26) has been determined. It reveals a 213-amino acid protein (27 kDa) that contains no methionine (Met) residues. Radiolabelling studies demonstrate the N-terminal Met residue is cleaved post-translationally. The Hsp26 amino acid sequence shows significant homology with both a range of eukaryotic small Hsps and with vertebrate alpha-crystallins. Particularly highly conserved among these proteins is a hydrophobic tetrapeptide sequence Gly-Val-Leu-Thr. These findings are discussed in relation to the structure and function of small Hsps.
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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Crystallins / genetics
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DNA, Fungal / genetics
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Fungal Proteins / biosynthesis
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Fungal Proteins / genetics*
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Fungal Proteins / physiology
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Genes, Fungal*
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Heat-Shock Proteins / biosynthesis
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Heat-Shock Proteins / genetics*
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Heat-Shock Proteins / physiology
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Humans
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Molecular Sequence Data
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Plants / genetics
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Plasmids
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Protein Biosynthesis
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RNA, Fungal / biosynthesis
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RNA, Fungal / genetics
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RNA, Messenger / biosynthesis
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RNA, Messenger / genetics
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Restriction Mapping
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Saccharomyces cerevisiae / genetics*
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Sequence Homology, Nucleic Acid
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Transcription, Genetic
Substances
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Crystallins
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DNA, Fungal
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Fungal Proteins
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Heat-Shock Proteins
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RNA, Fungal
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RNA, Messenger