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Gene Review

HBAD  -  alpha-D-globin

Gallus gallus

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Disease relevance of HBA2

  • To understand what role this splice sequence plays in the processing and maturation of nuclear RNA to cytoplasmic RNA, we have analyzed the intron processing of the alpha D-globin transcript in both heterologous (monkey) and homologous (chicken) cells using simian virus 40 and retrovirus vectors, respectively [1].

High impact information on HBA2

  • In both cell types, both introns of the alpha D-globin gene are efficiently and precisely removed [1].
  • We mapped at high resolution and as a function of development the hypersensitive domain in the 5'-flanking region of the chicken alpha D-globin gene and determined the specific protein-binding sites within the domain [2].
  • Comparison of our sequence data with the nucleotide sequence of the alpha D globin gene suggests that a single gene encodes both the embryonic and adult alpha D globin polypeptides [3].
  • Our results show that the overall genome organization is not disturbed in the immediate neighbourhood of the adult globin genes; the observed restriction fragments are identical for both DNAs after EcoRI, HindIII, BamHI and XbaI digestion, using the beta, alpha A and alpha D globin cDNA probes [4].
  • With respect to globin gene expression, however, we find that all but one of the globin genes studied (alpha D-globin) undergo dramatic developmental regulation [5].

Biological context of HBA2

  • The divergence between the alpha A and alpha D globin within a same species point to individual functional specificity and hence independent evolution and suggest that a mechanism of 'gene conversion' did not operate in between the avian alpha globin genes [6].
  • Screening of the DNA library resulted in the isolation of a recombinant, D alpha G-1, which carries both the adult duck alpha A- and alpha D-globin genes [7].
  • This silencer element can autonomously reduce the activity of promoters for thymidine kinase and alpha D globin [8].


  1. An unusual 5' splice sequence is efficiently utilized in vivo. Fischer, H.D., Dodgson, J.B., Hughes, S., Engel, J.D. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  2. Protein-binding sites within the 5' DNase I-hypersensitive region of the chicken alpha D-globin gene. Kemper, B., Jackson, P.D., Felsenfeld, G. Mol. Cell. Biol. (1987) [Pubmed]
  3. Minor early embryonic chick hemoglobin M. Amino acid sequences of the epsilon and alpha D chains. Chapman, B.S., Hood, L.E., Tobin, A.J. J. Biol. Chem. (1982) [Pubmed]
  4. Modification of the methylation pattern in the vicinity of the chicken globin genes in avian erythroblastosis virus transformed cells. Marcaud, L., Reynaud, C.A., Therwath, A., Scherrer, K. Nucleic Acids Res. (1981) [Pubmed]
  5. Developmental regulation of globin and nonglobin messenger RNAs in avian erythroid cells. Hansen, D.A., Seftor, E.A., DeKloe, J., McCabe, J.B., Tobin, A.J. Dev. Biol. (1984) [Pubmed]
  6. Determination of the primary sequence of the duck alpha D globin mRNA and comparison of all adult duck and chick globin mRNA sequences. Ben Tahar, S., Scherrer, K. Mol. Biol. Rep. (1983) [Pubmed]
  7. The isolation and partial characterization of linked alpha A- and alpha D-globin genes from a duck DNA recombinant library. Niessing, J., Erbil, C., Neubauer, V. Gene (1982) [Pubmed]
  8. Silencer and enhancer elements located at the 3'-side of the chicken and duck alpha-globin-encoding gene domains. Targa, F.R., de Moura Gallo, C.V., Huesca, M., Scherrer, K., Marcaud, L. Gene (1993) [Pubmed]
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