Search research articles

Search research articles

Related Experiment Videos

Classification and evolution of EF-hand proteins.

H Kawasaki¹, S Nakayama, R H Kretsinger

¹Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine

|April 7, 1999

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Mechanism of haematuria in lupus nephritis.

Annals of the rheumatic diseases·1995

Same author

[Prevalence and transmission of hepatitis C virus in polluted area in Japan].

Nihon rinsho. Japanese journal of clinical medicine·1995

Same author

[Changes of serum 2',5'-oligoadenylate synthetase activity and neopterin during interferon treatment for chronic hepatitis C].

Nihon rinsho. Japanese journal of clinical medicine·1995

Same author

Use of haloacetate dehalogenase genes as selection markers for Escherichia coli and Pseudomonas vectors.

Biodegradation·1995

Same author

Diagnosis of vascular compression in facial spasm by stereoscopic short-range magnetic resonance angiography. Technical note.

Journal of neurosurgery·1995

Same author

The effect of a TXA2 receptor antagonist ON-579 on experimental allergic reactions.

Prostaglandins, leukotrienes, and essential fatty acids·1995

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

This study identifies 45 EF-hand protein subfamilies, revealing evolutionary relationships and domain congruence. Thirteen CTER subfamilies evolved from a single ur-domain, while others show diverse evolutionary paths.

Area of Science:

Biochemistry
Molecular Biology
Evolutionary Biology

Background:

EF-hand proteins are crucial calcium-binding proteins involved in various cellular processes.
Understanding the evolutionary history and structural relationships of EF-hand protein subfamilies is essential for deciphering their functions.

Purpose of the Study:

To identify and classify distinct subfamilies of EF-hand proteins.
To investigate the evolutionary congruence and relationships among these subfamilies.
To explore the evolutionary origins and diversification of EF-hand protein domains.

Main Methods:

Analysis of amino acid sequences to identify EF-hand domains.
Construction of dendrograms to assess statistical similarity and congruence among domains.

Keywords:

NASA Discipline Exobiology Non-NASA Center

Related Experiment Videos

Comparative analysis of sequence and chemical characteristics across subfamilies and species.

Main Results:

Forty-five distinct EF-hand protein subfamilies were identified, each containing 2-8 EF-hand domains.
Thirteen subfamilies, collectively termed CTER (including Calmodulin and Troponin C), exhibit high congruence, suggesting a common evolutionary origin from a single ur-domain via gene duplication and fusion.
The remaining 32 subfamilies display less general congruence, with some forming distinct clusters (e.g., S100, calbindin 9 kd, trichohylin).
A pattern of ODD and EVEN domain similarity was observed across subfamilies.
Eighteen subfamilies are heterochimeric, containing additional domains of non-EF-hand origin.

Conclusions:

EF-hand protein evolution is characterized by both conserved duplication events (leading to CTER subfamilies) and more divergent evolutionary trajectories.
The identified subfamilies and their relationships provide a framework for understanding calcium signaling pathways.
Homoplasy is widespread, indicating convergent evolution of sequence and chemical characteristics.