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1

Thermodynamics of specific protein-RNA interactions.

100%

Stolarski R.

|

2003

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vol. 50

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issue 2

297-318

EN

Description of the recognition specificity between proteins and nucleic acids at the level of molecular interactions is one of the most challenging tasks in biophysics. It is key to understanding the course and control of gene expression and to the application of the thus acquired knowledge in chemotherapy. This review presents experimental results of thermodynamic studies and a discussion of the role of thermodynamics in formation and stability of functional protein-RNA complexes, with a special attention to the interactions involving mRNA 5' cap and cap-binding proteins in the initiation of protein biosynthesis in the eukaryotic cell. A theoretical framework for analysis of the thermodynamic parameters of protein-nucleic acid association is also briefly surveyed. Overshadowed by more spectacular achievements in structural studies, the thermodynamic investigations are of equal importance for full comprehension of biopolymers' activity in a quantitative way. In this regard, thermodynamics gives a direct insight into the energetic and entropic characteristics of complex macromolecular systems in their natural environment, aqueous solution, and thus complements the structural view derived from X-ray crystallography and multidimensional NMR. Further development of the thermodynamic approach toward interpretation of recognition and binding specificity in terms of molecular biophysics requires more profound contribution from statistical mechanics.

2

Acyclonucleosides: Acyclobenzimidazole nucleoside and nucleotide analogues and conformations of the acyclic chains by means of NMR spectroscopy

51%

Kazimierczuk Z., Stolarski R., Shugar D.

Acta Biochimica Polonica

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1984

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vol. 31

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issue 1

33-48

3

Cyclic phosphates of some antiviral acyclonucleosides: relationship between conformation and substrate/inhibitor properties in some enzyme systems

51%

Cieśla J. M., Stolarski R., Shugar D.

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vol. 40

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issue 2

251-260

4

Hydroxylamine and methoxyamine mutagenesis: Tautomeric equilibrium of the promutagenic analogue, N^6-methoxyadenosine, in solvents of different polarities

51%

Kierdaszuk B., Stolarski R., Shugar D.

Acta Biochimica Polonica

|

1984

|

vol. 31

|

issue 1

49-64

5

Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues.

33%

Stachelska A., Wieczorek Z., Ruszczyńska K., Stolarski R., Pietrzak M., Lamphear B. J., Rhoads R. E., Darżynkiewicz E., Jankowska-Anyszka M.

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2002

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vol. 49

|

issue 3

671-682

EN

Translation initiation factor eIF4E binds the m7G cap of eukaryotic mRNAs and mediates recruitment of mRNA to the ribosome during cap-dependent translation initiation. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m32,2,7G, which is poorly recognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m7GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m7G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m7G- and m32,2,7G-containing caps (Kas 2×106 M-1 to 7×106 M-1) whereas IFE-3 and IFE-4 discriminated strongly in favor of m7G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of Kas on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.

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Thermodynamics of specific protein-RNA interactions.

Acyclonucleosides: Acyclobenzimidazole nucleoside and nucleotide analogues and conformations of the acyclic chains by means of NMR spectroscopy

Cyclic phosphates of some antiviral acyclonucleosides: relationship between conformation and substrate/inhibitor properties in some enzyme systems

Hydroxylamine and methoxyamine mutagenesis: Tautomeric equilibrium of the promutagenic analogue, N^6-methoxyadenosine, in solvents of different polarities

Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues.