Impaired interaction of α-haemoglobin-stabilising protein with α-globin termination mutant in a yeast two-hybrid system
Chairat Turbpaiboon
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorThawornchai Limjindaporn
Department of Anatomy, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorWiyada Wongwiwat
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorYaowalak U-Pratya
Division of Hematology, Department of Medicine, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand
Search for more papers by this authorNoppadol Siritanaratkul
Division of Hematology, Department of Medicine, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand
Search for more papers by this authorPa-thai Yenchitsomanus
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorSarawut Jitrapakdee
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Search for more papers by this authorPrapon Wilairat
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Search for more papers by this authorChairat Turbpaiboon
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorThawornchai Limjindaporn
Department of Anatomy, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorWiyada Wongwiwat
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorYaowalak U-Pratya
Division of Hematology, Department of Medicine, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand
Search for more papers by this authorNoppadol Siritanaratkul
Division of Hematology, Department of Medicine, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand
Search for more papers by this authorPa-thai Yenchitsomanus
Medical Molecular Biology Unit, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Department of Immunology, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok
Search for more papers by this authorSarawut Jitrapakdee
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Search for more papers by this authorPrapon Wilairat
Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok
Search for more papers by this authorSummary
α-Thalassaemia caused by α-globin gene termination codon mutations (αT-globin) has been explained by their inherent mRNA instability and by oxidative damage arising from the presence of membrane-bound αT-globin chains. To better understand the latter phenomenon, a yeast two-hybrid system was used to assay the interaction between αT-globin and its molecular chaperone, α-haemoglobin-stabilising protein (AHSP) and impaired binding of αT-globin with AHSP compared with αwild-type-globin was observed.
References
- Estojak, J., Brent, R. & Golemis, E.A. (1995) Correlation of two-hybrid affinity data with in vitro measurements. Molecular and Cellular Biology, 15, 5820–5829.
- Feng, L., Gell, D.A., Zhou, S., Gu, L., Kong, Y., Li, J., Hu, M., Yan, N., Lee, C., Rich, A.M., Armstrong, R.S., Lay, P.A., Gow, A.J., Weiss, M.J., Mackay, J.P. & Shi, Y. (2004) Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin. Cell, 119, 629–640.
- Feng, L., Zhou, S., Gu, L., Gell, D.A., Mackay, J.P., Weiss, M.J., Gow, A.J. & Shi, Y. (2005) Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem. Nature, 435, 697–701.
- Fucharoen, S. & Winichagoon, P. (1987) Hemoglobinopathies in Southeast Asia. Hemoglobin, 11, 65–88.
- Fucharoen, S., Winichagoon, P., Pootrakul, P., Piankijagum, A. & Wasi, P. (1987) Differences between two types of Hb H disease, alpha-thalassemia 1/alpha-thalassemia 2 and alpha-thalassemia 1/Hb constant spring. Birth Defects Original Article Series, 23, 309–315.
- Gell, D., Kong, Y., Eaton, S.A., Weiss, M.J. & Mackay, J.P. (2002) Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein. Journal of Biological Chemistry, 277, 40602–40609.
- Golemis, E.A., Serebriiskii, I., Finley, R.L., Kolonin, M.G., Gyuris, J. & Brent, R. (1999) Interaction trap/two-hybrid system to identify interacting proteins. In: Current Protocols in Molecular Biology (ed. by F.M. Ausubel, R Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl), pp. 20.1.1–20.1.40. John Wiley & Sons, New Jersey, USA.
- Kong, Y., Zhou, S., Kihm, A.J., Katein, A.M., Yu, X., Gell, D.A., Mackay, J.P., Adachi, K., Foster-Brown, L., Louden, C.S., Gow, A.J. & Weiss, M.J. (2004) Loss of alpha-hemoglobin-stabilizing protein impairs erythropoiesis and exacerbates beta-thalassemia. Journal of Clinical Investigation, 114, 1457–1466.
- Peerapittayamongkol, C., Bernini, L.F. & Wilairat, P. (1996) Presence of αCS-globin on membrane of red cells containing hemoglobin constant spring (CS). Journal of the Science Society of Thailand, 22, 117–120.
- Schrier, S.L., Bunyaratvej, A., Khuhapinant, A., Fucharoen, S., Aljurf, M., Snyder, L.M., Keifer, C.R., Ma, L. & Mohandas, N. (1997) The unusual pathobiology of hemoglobin constant spring red blood cells. Blood, 89, 1762–1769.
- Turbpaiboon, C., Siritantikorn, A., Thongnoppakhun, W., Bunditworapoom, D., Limwongse, C., Yenchitsomanus, P.T., Siritanaratkul, N. & Wilairat, P. (2004) Hemoglobin Pakse: presence on red blood cell membrane and detection by polymerase chain reaction-single-strand conformational polymorphism. International Journal of Hematology, 80, 136–139.
- Viprakasit, V., Tanphaichitr, V.S., Pung-Amritt, P., Petrarat, S., Suwantol, L., Fisher, C. & Higgs, D.R. (2002) Clinical phenotypes and molecular characterization of Hb H-Pakse disease. Haematologica, 87, 117–125.
- Weiss, I.M. & Liebhaber, S.A. (1994) Erythroid cell-specific determinants of alpha-globin mRNA stability. Molecular and Cellular Biology, 14, 8123–8132.
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