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Published on: January 22, 2020
Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution
Mikhail L Kuravsky1, Vladimir V Aleshin, Dmitrij Frishman
1Faculty of Bioengineering and Bioinformatics, MV Lomonosov Moscow State University, Moscow, Russian Federation.
BMC Evolutionary Biology
|June 14, 2011
Summary
Glyceraldehyde-3-phosphate dehydrogenase-2 (GAPD-2) evolved from a gene duplication in early chordates and specialized in mammals and lizards. This testis-specific protein gained a proline-rich domain for sperm tail binding, likely from a microsatellite region.
Area of Science:
- Evolutionary biology
- Biochemistry
- Genomics
Background:
- Glyceraldehyde-3-phosphate dehydrogenase (GAPD) has glycolytic and non-glycolytic functions.
- Two mammalian isoenzymes exist: GAPD-1 (somatic) and GAPD-2 (testis-specific).
- GAPD-2's unique N-terminal proline-rich domain aids sperm tail cytoskeleton binding.
Purpose of the Study:
- Investigate the evolutionary history of GAPD isoenzymes.
- Understand the specialization of GAPD-2 as a testis-specific protein.
Main Methods:
- Assembled a dataset of GAPD sequences from public databases.
- Reconstructed phylogeny using Bayesian methods.
- Performed syntenic analysis and selection tests for precise evolutionary insights.
Main Results:
- GAPD-1 and GAPD-2 originated from a gene duplication early in chordate evolution.
- GAPD-2 was lost in most lineages, persisting in lizards, mammals, and fish.
- Selective pressures varied across lineages, isoenzymes, and sequence regions.
Conclusions:
- In reptiles and mammals, GAPD-2 specialized for testis function, acquiring a proline-rich domain likely from a microsatellite region.
- This domain anchors GAPD-2 to the sperm tail cytoskeleton.
- Lizard GAPD-2, found in regenerating tissues, lacks this domain due to alternative splicing.
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