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Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons196902

Divita,  Gilles
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons117920

Restle,  Tobias
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93142

Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Divita, G., Restle, T., & Goody, R. S. (1993). Characterization of the dimerization process of HIV-1 reverse transcriptase heterodimer using intrinsic protein fluorescence. FEBS Letters, 324(2), 153-158. doi:10.1016/0014-5793(93)81383-B.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0019-AA41-C
Zusammenfassung
Intrinsic protein fluorescence has been used to study dimerization of the HIV-1 reverse transcriptase (RT). We observed a 25% increase of the tryptophan fluorescence of the enzyme during dissociation of the subunits induced by the addition of acetonitrile. Upon reassociation of the separated subunits, the original fluorescence emission of the heterodimer is restored. A two-state transition model for the RT dimerization process in which the dimers are in equilibrium with folded monomers is proposed. The free energy of dissociation was determined to be 12.2 (± 0.2) kcal/mol. In the absence of Mg2+ ions a decrease of this value was observed, whereas the addition of a synthetic primer/template (18/36mer) results in an increase of dimer stability. Analyzing the effect of Mg2+ on the establishment of the binding equilibrium, a dramatic effect with a 100-fold acceleration of the association by the divalent ion was observed.