A spectroscopic study of the binding of m7GTP and m7GpppG to human protein synthesis initiation factor 4E

Carberry, Susan E.; Rhoads, Robert E.; Goss, Dixie J.

doi:10.1021/bi00446a017

Cited by 88 publications

(89 citation statements)

References 40 publications

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“…[25], due to sandwich stacking between 7-methylguanine and two tryptophan indole rings [20,23]. The titration experiments were carried out in 50 mM Hepes/KOH (pH 7.2), 1 mM DTT, 0.5 mM EDTA and appropriate amount of KCl.…”

Section: 1mentioning

confidence: 99%

Poisson–Boltzmann model analysis of binding mRNA cap analogues to the translation initiation factor eIF4E

Szklarczyk

Zuberek

Antosiewicz

2009

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT AbstractThe electrostatic free energy of binding of two analogues of the 5'-mRNA cap, differing in size and electric charge, to the wild type and mutated eukaryotic initiation factor eIF4E was computed using the finite difference solutions to the Poisson-Boltzmann equation. Two definitions of the solute-solvent dielectric boundary were used: van der Waals model, solvent exclusion (SE) model. The computed electrostatic energies were supplemented by estimations of the non polar and entropic contributions. A comparison with experimental data for the investigated systems was done. It appears that the SE model with additional contribution fits experimental findings better than the van der Waals model does.

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Section: 1mentioning

confidence: 99%

Poisson–Boltzmann model analysis of binding mRNA cap analogues to the translation initiation factor eIF4E

Szklarczyk

Zuberek

Antosiewicz

2009

Biophysical Chemistry

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“…analogues. The observed signal decay results from the protein's tryptophan fluorescence quenching accompanying the formation of the complex [8]. It can be noted that quenching is the smallest and slowest for m 7 GMP, and the largest and fastest for m 7 GTP, and that with an increasing concentration of the ligand, a smaller part of the binding reaction is visible in the kinetic traces.…”

Section: Analysis Of the Experimental Datamentioning

confidence: 94%

“…[8], due to sandwich stacking between 7-methylguanine and two tryptophan indole rings [4,7]. Measurements were done using a SX.18MV stopped-flow reaction analyser from Applied Photophysics Ltd.…”

Section: Stopped-flow Measurements and Analysis Of The Experimental Datamentioning

confidence: 99%

“…The interaction energies also include contributions due to shifts in the appropriate pK a values upon binding. These insights into structural characteristics of cap-eIF4E complexes were obtained from three-dimensional structures by x-ray crystallography [4][5][6] and multidimensional NMR study [7], as well as from spectroscopic investigations in vitro, both equilibrium [5,8,9], and kinetic [10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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Kinetics of binding the mRNA cap analogues to the translation initiation factor eIF4E under second-order reaction conditions

Błachut-Okrasińska¹,

Bojarska²,

Stępiński³

et al. 2007

Biophysical Chemistry

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of binding the mRNA cap analogues to the translation initiation factor eIF4E under second-order reaction conditions. Biophysical Chemistry, Elsevier, 2007, 129 (2-3) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. The kinetics of binding of five analogues of the 5'-mRNA cap, di ering in size and electric charge, to the eukaryotic initiation factor eIF4E, at 20 • C, pH 7.2, and ionic strength of 150 mM, were measured, after mixing solutions of comparable concentrations of the reagents, in a stopped-flow spectrofluorimeter. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPTThe registered stopped-flow signals were fitted using an e cient software package, called Dyna Fit, based on a numerical solution of the kinetic rate equations for assumed reaction mechanisms. One-, two-, and three-step binding models were considered. The quality of fits for these models were compared using two statistical criteria: Akaike's Information Criterion and Bayesian Information Criterion. Based on resulting probabilities of the models, it was concluded that for all investigated ligands a one-step binding model has essentially no support in the experimental observations. Our conclusions were also analysed from the perspective of kinetic transients obtained for cap-eIF4E systems under the so called pseudo-first order reaction condition, which result in the linear correlation of the observed association rate constant with ligand concentration. The existence of such a linear correlation is usually considered as proof of a one step binding mechanism. The kinetic and optical parameters, derived from fitting a two-step cap binding model with the DynaFit, were used to simulate kinetic transients under pseudo-first order reaction conditions. It appeared that the observed association rate constants derived from these simulated transients are also linearly correlated with the ligand concentration. This indicated that these linear dependencies are not su cient to conclude a one-step binding.

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“…[151][152][153] TMG-capped-RNAs are known to translate poorly, 154 due to the inefficient recognition of the trimethyl by the cap-binding protein eIF4E. [155][156][157][158] As a consequence, it would be predicted that TMG-HIV-1 RNAs would be inefficiently translated resulting in a decrease of viral expression. However, this is not the case and TMG-capping of viral mRNAs associates with an increased expression of HIV-1 structural proteins.…”

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confidence: 99%

Translation initiation of the HIV-1 mRNA

Ohlmann¹,

Mengardi²,

López-Lastra³

2014

translation

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Translation initiation of the full-length mRNA of the human immunodeficiency virus can occur via several different mechanisms to maintain production of viral structural proteins throughout the replication cycle. HIV-1 viral protein synthesis can occur by the use of both a capdependant and IRES-driven mechanism depending on the physiological conditions of the cell and the status of the ongoing infection. For both of these mechanisms there is a need for several viral and cellular co-factors for optimal translation of the viral mRNA. In this review we will describe the mechanism used by the full-length mRNA to initiate translation highlighting the role of co-factors within this process. A particular emphasis will be given to the role of the DDX3 RNA helicase in HIV-1 mRNA translation initiation.

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A spectroscopic study of the binding of m7GTP and m7GpppG to human protein synthesis initiation factor 4E

Cited by 88 publications

References 40 publications

Poisson–Boltzmann model analysis of binding mRNA cap analogues to the translation initiation factor eIF4E

Poisson–Boltzmann model analysis of binding mRNA cap analogues to the translation initiation factor eIF4E

Kinetics of binding the mRNA cap analogues to the translation initiation factor eIF4E under second-order reaction conditions

Translation initiation of the HIV-1 mRNA

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