Impaired interaction of alpha-haemoglobin-stabilising protein with alpha-globin termination mutant in a yeast two-hybrid system.
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.
Turbpaiboon
Chairat
C
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand.
Limjindaporn
Thawornchai
T
Wongwiwat
Wiyada
W
U-Pratya
Yaowalak
Y
Siritanaratkul
Noppadol
N
Yenchitsomanus
Pa-thai
PT
Jitrapakdee
Sarawut
S
Wilairat
Prapon
P
D001798:Blood Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D015870:Gene Expression / Q000235:genetics; D005914:Globins / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D010641:Phenotype; D011485:Protein Binding; D012333:RNA, Messenger / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D017085:alpha-Thalassemia / Q000235:genetics / Q000378:metabolism
C468768:AHSP protein, human; D001798:Blood Proteins; D018832:Molecular Chaperones; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; D005914:Globins