Open AccessMouse IgA heavy chain gene sequence: implications for evolution of immunoglobulin hinge axons.
Author(s) -
Philip W. Tucker,
Jerry L. Slightom,
Frederick R. Blattner
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.12.7684
Subject(s) - exon , coding region , gene , immunoglobulin heavy chain , microbiology and biotechnology , alpha chain , splice , antibody , biology , hinge , alpha (finance) , nucleic acid sequence , gene duplication , immunoglobulin light chain , genetics , physics , medicine , construct validity , nursing , classical mechanics , patient satisfaction
The complete nucleotide sequence of the gene and mRNA coding for the constant (C) region of the secreted form of the BALB/c mouse IgA immunoglobulin alpha heavy (H) chain has been determined. As in other immunoglobulins, the three C region domains of the alpha protein, C alpha 1, C alpha 2, and C alpha 3 are coded in separate exons. However, the hinge region of C alpha is not coded on a separate exon as it is in other hinge-containing immunoglobulins. Instead, the alpha hinge is coded as a 5' extension of the C alpha 2 exon, and we suggest that it may have evolved by duplication leading to incorporation of an acceptor RNA splice site into the coding portion of the C alpha 2 exon. Extensions of this concept could provide an explanation for duplications in the human alpha 1 chain.