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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AA41-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2736-8
Genre: Journal Article

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FEBSLett_324_1993_153.pdf (Any fulltext), 673KB
 
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 Creators:
Divita, Gilles1, Author              
Restle, Tobias1, 2, 3, Author              
Goody, Roger S.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              
3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: HIV; Reverse transcriptase; Dimerization; Intrinsic protein fluorescence; Gdn-HCl, guanidinium hydrochloride; HIV, human immunodeficiency virus; HPLC, high-performance liquid chromatography; RT, reverse transcriptase
 Abstract: 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.

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Language(s): eng - English
 Dates: 1993-04-131993-04-222001-11-051993-06-14
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 324 (2) Sequence Number: - Start / End Page: 153 - 158 Identifier: ISSN: 0014-5793
CoNE: /journals/resource/954925399501