Abstract
Alpha-thalassaemia caused by alpha-globin gene termination codon mutations (alphaT-globin) has been explained by their inherent mRNA instability and by oxidative damage arising from the presence of membrane-bound alphaT-globin chains. To better understand the latter phenomenon, a yeast two-hybrid system was used to assay the interaction between alphaT-globin and its molecular chaperone, alpha-haemoglobin-stabilising protein (AHSP) and impaired binding of alphaT-globin with AHSP compared with alpha(wild-type)-globin was observed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Blood Proteins / genetics*
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Blood Proteins / metabolism
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Cloning, Molecular
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Gene Expression / genetics
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Globins / genetics*
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Globins / metabolism
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Humans
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Molecular Chaperones / genetics*
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Molecular Chaperones / metabolism
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Mutation
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Phenotype
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Protein Binding
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RNA, Messenger / genetics
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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alpha-Thalassemia / genetics
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alpha-Thalassemia / metabolism
Substances
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AHSP protein, human
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Blood Proteins
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Molecular Chaperones
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RNA, Messenger
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Saccharomyces cerevisiae Proteins
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Globins