Evolution of the Antarctic teleost immunoglobulin heavy chain gene

Notothenioid teleosts underwent major modifications of their genome to adapt to the cooling of the Antarctic environment. In order to identify specific features of the Antarctic teleost immunoglobulin, transcripts encoding the constant region of the IgM heavy chain from 13 Antarctic and non-Antarcti...

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Bibliographic Details
Published in:Molecular phylogenetics and evolution 2010-04, Vol.55 (1), p.226-233
Main Authors: Coscia, Maria Rosaria, Varriale, Sonia, De Santi, Concetta, Giacomelli, Stefano, Oreste, Umberto
Format: Article
Language:English
Subjects:
Alternative mRNA splicing
Amino acids
Animals
Antarctic teleost evolution
Antarctica
Base Sequence
Chains
Cold adaptation
Cold Temperature
Computational Biology
Encoding
Evolution
Evolution, Molecular
Exons
Fishes - classification
Fishes - genetics
Genes, Immunoglobulin Heavy Chain
Genomes
Immunoglobulin gene structure
Immunoglobulin Heavy Chains - genetics
Immunoglobulin M - genetics
Immunoglobulins
Inclusions
Models, Genetic
Models, Molecular
Molecular Sequence Data
Notothenioidei
RNA Splicing
Sequence Alignment
Sequence Analysis, DNA
Teleostei
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Summary:Notothenioid teleosts underwent major modifications of their genome to adapt to the cooling of the Antarctic environment. In order to identify specific features of the Antarctic teleost immunoglobulin, transcripts encoding the constant region of the IgM heavy chain from 13 Antarctic and non-Antarctic notothenioid species were sequenced. The primary mRNA splicing for the membrane form was found to be atypical in the majority of Antarctic species, because it led to exclusion of two entire constant exons, and to inclusion of 39-nucleotide exons encoding an unusually long Extracellular Membrane-Proximal Domain (EMPD). Genomic DNA analysis revealed that each 39-nucleotide exon fell within a long sequence that was the reverse complement of an upstream region. Deduced amino acid sequence analysis lead to the identification of cysteine encoding codons in the 39-nucleotide exons, but not in the respective sequence counterpart, suggesting that these residues might play an important role in the folding of the EMPD.
ISSN:1055-7903
1095-9513
DOI:10.1016/j.ympev.2009.09.033