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Nucleic Acids Research, 1990, Vol. 18, No. 17 5227-5233
© 1990

MOLECULAR BIOLOGY

The immunoglobulin M heavy chain constant region gene of the channel catfish, Ictalurus punctatus: an unusual mRNA splice pattern produces the membrane form of the molecule

Melanie R. Wilson, Ann Marcuz, Frederick van Ginkel1, Norman W. Miller1, L. William Clem1, Darlene Middleton2 and Gregory W. Warr2,*

Basel Institute for Immunology Grenzacherstrasse 487, CH-4005 Basel, Switzerland 1Department of Microbiology, University of Mississippi Medical Center Jackson, MS 39216 2Department of Biochemistry and Molecular Biology, Medical University of South Carolina 171 Ashley Avenue, Charleston, SC 29425, USA

*To whom correspondence should be addressed

Received May 2, 1990. Revised July 26, 1990. Accepted July 26, 1990.

The immunoglobulin (IgM) heavy chain constant region gene of the channel catfish, Ictalurus punctatus, has been cloned and characterized. The gene contains four constant region domain-encoding exons (CH1 to CH4) expressed in the secreted form of the immunoglobulin, and two exons encoding the transmembrane (TM) domain utilized in the lymphocyte membrane receptor form of the Immunoglobulin. The sequence of a cDNA clone encoding the 3' region of the message for the membrane receptor form of the µ chain indicates that the TM1 exon is spliced directly to the CH3 exon, and not into a site within the CH4 exon, as occurs in the mammals, a shark and an amphibian. This unusual pattern of splicing, which produces a membrane heavy chain that is characteristically smaller than the secreted heavy chain, may be common to all teleost fish.


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