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. 1981 Aug;78(8):4796–4800. doi: 10.1073/pnas.78.8.4796

Theoretical aspects of translocation on DNA: adenosine triphosphatases and treadmilling binding proteins.

T L Hill, T Tsuchiya
PMCID: PMC320250  PMID: 6272273

Abstract

The basic kinetic and bioenergetic theory is outlined for two kinds of translocation on DNA: (i) helicases that use ATP to move along single-stranded DNA or to move on and invade double-stranded DNA at a replication fork; and (ii) DNA-binding proteins (not ATPases) that form bound aggregates on single-stranded DNA and facilitate replication by steady-state treadmilling of molecules between the ends of the aggregate. The respective resemblances to myosin--actin in muscle and to steady-state treadmilling in solution of actin or tubulin are pointed out.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bergen L. G., Borisy G. G. Head-to-tail polymerization of microtubules in vitro. Electron microscope analysis of seeded assembly. J Cell Biol. 1980 Jan;84(1):141–150. doi: 10.1083/jcb.84.1.141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Das R. H., Yarranton G. T., Gefter M. L. Enzyme-catalyzed DNA unwinding. The role of ATP in helicase III activity. J Biol Chem. 1980 Sep 10;255(17):8069–8073. [PubMed] [Google Scholar]
  3. Eisenberg E., Hill T. L., Chen Y. Cross-bridge model of muscle contraction. Quantitative analysis. Biophys J. 1980 Feb;29(2):195–227. doi: 10.1016/S0006-3495(80)85126-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hill T. L. Bioenergetic aspects and polymer length distribution in steady-state head-to-tail polymerization of actin or microtubules. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4803–4807. doi: 10.1073/pnas.77.8.4803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hill T. L. Steady-state head-to-tail polymerization of actin or microtubules. II. Two-state and three-state kinetic cycles. Biophys J. 1981 Mar;33(3):353–371. doi: 10.1016/S0006-3495(81)84900-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
  7. Kirschner M. W. Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo. J Cell Biol. 1980 Jul;86(1):330–334. doi: 10.1083/jcb.86.1.330. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Margolis R. L., Wilson L. Addition of colchicine--tubulin complex to microtubule ends: the mechanism of substoichiometric colchicine poisoning. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3466–3470. doi: 10.1073/pnas.74.8.3466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Wegner A. Head to tail polymerization of actin. J Mol Biol. 1976 Nov;108(1):139–150. doi: 10.1016/s0022-2836(76)80100-3. [DOI] [PubMed] [Google Scholar]
  10. Yarranton G. T., Gefter M. L. Enzyme-catalyzed DNA unwinding: studies on Escherichia coli rep protein. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1658–1662. doi: 10.1073/pnas.76.4.1658. [DOI] [PMC free article] [PubMed] [Google Scholar]

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