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Related Experiment Videos

Phosphagen kinase evolution. Expression in echinoderms.

A Ratto1, B M Shapiro, R Christen

  • 1Unité associée 671 du Centre National de la Recherche Scientifique, Station Zoologique, Villefranche-sur-mer, France.

European Journal of Biochemistry
|December 8, 1989
PubMed
Summary
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Echinoderms uniquely possess both arginine kinase and creatine kinase, enzymes crucial for cellular energy. This study reveals distinct molecular structures for these kinases across echinoderm classes, offering evolutionary insights.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Arginine kinase and creatine kinase are vital for cellular energetics, transferring phosphate groups.
  • Most animals have one primary phosphagen kinase (creatine kinase in chordates, arginine kinase in protostomes).
  • Echinoderms uniquely exhibit both arginine kinase and creatine kinase activities, sometimes within the same tissue.

Purpose of the Study:

  • To investigate the expression and molecular characteristics of arginine kinase and creatine kinase across the five extant classes of echinoderms.
  • To determine the native molecular masses and subunit compositions of these enzymes in different echinoderm tissues.
  • To discuss the developmental and evolutionary implications of the distinct phosphagen kinase structures found in echinoderms.

Main Methods:

Related Experiment Videos

  • Gel filtration chromatography to ascertain the native molecular masses of the enzymes.
  • SDS-PAGE and Western blotting with specific antibodies to analyze subunit composition.
  • Analysis of echinoderms from five classes: echinoids, asteroids, ophiuroids, holothurians, and crinoids.

Main Results:

  • Arginine kinase consistently appeared as an ~81 kDa dimer composed of two 42 kDa subunits in all analyzed echinoderms.
  • Creatine kinase was found to be a monomeric enzyme with molecular masses ranging from 140-155 kDa across echinoderms.
  • Distinct molecular structures were observed for arginine kinase (dimeric) and creatine kinase (monomeric) in echinoderms, differing from other animal groups.

Conclusions:

  • Echinoderms possess both arginine kinase and creatine kinase with unique, conserved molecular structures.
  • The dimeric nature of echinoderm arginine kinase and monomeric creatine kinase suggests specific adaptations.
  • These findings provide insights into the evolutionary diversification of phosphagen kinase systems in marine invertebrates.