Literature DB >> 18615236

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

J Gardiner1, P McGee, R Overall, J Marc.   

Abstract

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.

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Year:  2008        PMID: 18615236     DOI: 10.1007/s00709-008-0305-z

Source DB:  PubMed          Journal:  Protoplasma        ISSN: 0033-183X            Impact factor:   3.356


  71 in total

1.  Cooperative symmetry-breaking by actin polymerization in a model for cell motility.

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Journal:  Nat Cell Biol       Date:  1999-12       Impact factor: 28.824

2.  Scaling of microtubule force-velocity curves obtained at different tubulin concentrations.

Authors:  Marcel E Janson; Marileen Dogterom
Journal:  Phys Rev Lett       Date:  2004-06-16       Impact factor: 9.161

Review 3.  Biomimetic actuators: where technology and cell biology merge.

Authors:  M Knoblauch; W S Peters
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Review 4.  The tubulin code.

Authors:  Kristen J Verhey; Jacek Gaertig
Journal:  Cell Cycle       Date:  2007-06-26       Impact factor: 4.534

5.  The interaction of actin filaments with microtubules and microtubule-associated proteins.

Authors:  L M Griffith; T D Pollard
Journal:  J Biol Chem       Date:  1982-08-10       Impact factor: 5.157

6.  G-actin-tubulin interaction.

Authors:  A B Verkhovsky; I G Surgucheva; V I Gelfand; V A Rosenblat
Journal:  FEBS Lett       Date:  1981-12-07       Impact factor: 4.124

7.  The nuclear actin-related protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones.

Authors:  M Harata; Y Oma; S Mizuno; Y W Jiang; D J Stillman; U Wintersberger
Journal:  Mol Biol Cell       Date:  1999-08       Impact factor: 4.138

8.  Characterization of MAP1B heavy chain interaction with actin.

Authors:  N Cueille; C Tallichet Blanc; S Popa-Nita; S Kasas; S Catsicas; G Dietler; B M Riederer
Journal:  Brain Res Bull       Date:  2007-01-03       Impact factor: 4.077

9.  Interaction of microtubule-associated protein 2 with actin filaments.

Authors:  R F Sattilaro
Journal:  Biochemistry       Date:  1986-04-22       Impact factor: 3.162

10.  Dynamic relocalization of histone MacroH2A1 from centrosomes to inactive X chromosomes during X inactivation.

Authors:  T P Rasmussen; M A Mastrangelo; A Eden; J R Pehrson; R Jaenisch
Journal:  J Cell Biol       Date:  2000-09-04       Impact factor: 10.539

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