Open Access Research article

Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution

Mikhail L Kuravsky1, Vladimir V Aleshin23, Dmitrij Frishman4* and Vladimir I Muronetz12*

Author Affiliations

1 Faculty of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, Leninskiye Gory 1-73, Moscow 119991, Russian Federation

2 A.N. Belozersky Institute for Physical and Chemical Biology, M.V. Lomonosov Moscow State University, Leninskiye Gory 1-40, Moscow 119991, Russian Federation

3 Kharkevich Institute for Information Transmission Problems of the Russian Academy of Sciences, Moscow, 127994, Russian Federation

4 Department of Genome Oriented Bioinformatics, Technische Universität München, Wissenschaftszentrum Weihenstephan, Freising 85354, Germany

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BMC Evolutionary Biology 2011, 11:160  doi:10.1186/1471-2148-11-160

Published: 10 June 2011

Additional files

Additional file 1:

Alignment of the two forms of Anolis carolinensis GAPD-2 mRNA. The sequence of protein product is represented; the possible start codons are in bold. Translation of the full-length mRNA seems to begin from the first start codon and the protein product will possess the proline-rich domain (shown in italic). The shortened mRNA lacks the first start codon. Therefore translation should begin from the second one resulting in a protein product without the proline-rich domain.

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Additional file 2:

The proline-rich N-terminal domains of mammalian GAPD-2.

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Additional file 3:

Accession codes of GAPD sequences used in the analysis.

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Additional file 4:

Raw alignment of GAPD nucleic sequences used in the phylogenetic analysis.

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