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Related Experiment Video

Updated: Jun 2, 2026

Dissection and Flat-mounting of the Threespine Stickleback Branchial Skeleton

Dissection and Flat-mounting of the Threespine Stickleback Branchial Skeleton

Published on: May 7, 2016

Tracing protein evolution through ancestral structures of fish galectin.

Ayumu Konno¹, Atsushi Kitagawa, Mizuki Watanabe

¹Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University, Sendai 980-8577, Japan.

Structure (London, England : 1993)

|May 14, 2011

Summary

Ancestral fish galectins reveal rapid evolution and differentiation in biological defense proteins. Natural selection shaped congerin structure and function, enhancing cytotoxic activity and carbohydrate specificity.

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Dissection and Flat-mounting of the Threespine Stickleback Branchial Skeleton

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Area of Science:

Biochemistry
Evolutionary Biology
Structural Biology

Background:

Fish galectins, known as congerins, are key components of the biological defense system.
Extant isoforms I and II of congerin have undergone rapid differentiation due to natural selection.

Purpose of the Study:

To determine the ancestral structures of fish galectins (congerins).
To elucidate the evolutionary path and differentiation mechanisms of congerins under selection pressure.

Main Methods:

Comparative structural analysis of ancestral and extant congerin isoforms.
Determination of ancestral congerin dimer structure.
Functional analyses of cytotoxic activity and carbohydrate binding.

Main Results:

The ancestral congerin structure exhibited intermediate features of extant isoforms I and II.
Protein-fold evolution was specific to the congerin I lineage and not present in the ancestor.
Differences in dimer interface and carbohydrate-binding sites suggest selection for stability and specificity.
Ancestral congerins displayed lower cytotoxic activity compared to their descendants.

Conclusions:

Ancestral congerin structure provides insights into the evolutionary divergence of fish galectins.
Natural selection has driven significant changes in congerin structure, function, and specificity.
Atomic-level details reveal the evolutionary process of protein differentiation in defense systems.