, Volume 233, Issue 1, pp 1–5

Are histones, tubulin, and actin derived from a common ancestral protein?

New Ideas in Cell Biology

DOI: 10.1007/s00709-008-0305-z

Cite this article as:
Gardiner, J., McGee, P., Overall, R. et al. Protoplasma (2008) 233: 1. doi:10.1007/s00709-008-0305-z


Histones and the cytoskeletal components tubulin and actin all act as thermal ratchets, using the energy present in Brownian motion to do work. All three also bind to nucleotides. Here we suggest that histones, tubulin, and actin derive from a common ancestral protein. There is some sequence similarity between histone 2A and the bacterial tubulin homologue FtsZ. Histones and actin also share some sequence similarity in the nucleotides and at phosphate-binding sites. Thus, actin and tubulin may also be related, although this is not obvious from sequence analysis. Indeed, actin and tubulin are closely functionally related and cooperate in many cellular processes. Interestingly, recent advances in nanotechnology suggest that thermal ratchets may be able to impart lifelike properties; thus, the evolution of the ancestral histone, tubulin, and actin thermal ratchet may have been crucial in the development of complexity in living organisms.

Keywords: Histone; Tubulin; Actin; Thermal ratchet; Cytoskeleton. 

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  1. 1.School of Biological SciencesUniversity of SydneyCamperdown

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