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Biophysical Journal 85:3587-3599 (2003)
© 2003 The Biophysical Society

A Perspective on Mechanisms of Protein Tetramer Formation

Evan T. Powers * and David L. Powers {dagger}

* Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037; and {dagger} Department of Mathematics and Computer Science, Clarkson University, Potsdam, New York 13699

Correspondence: Address reprint requests to E. T. Powers, Tel.: 858-784-9607; Fax: 858-784-9611; E-mail: epowers{at}scripps.edu.

Homotetrameric proteins can assemble by several different pathways, but have only been observed to use one, in which two monomers associate to form a homodimer, and then two homodimers associate to form a homotetramer. To determine why this pathway should be so uniformly dominant, we have modeled the kinetics of tetramerization for the possible pathways as a function of the rate constants for each step. We have found that competition with the other pathways, in which homotetramers can be formed either by the association of two different types of homodimers or by the successive addition of monomers to homodimers and homotrimers, can cause substantial amounts of protein to be trapped as intermediates of the assembly pathway. We propose that this could lead to undesirable consequences for an organism, and that selective pressure may have caused homotetrameric proteins to evolve to assemble by a single pathway.




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