Literature DB >> 20589527

Comparison of EMSA and SPR for the characterization of RNA-RNase II complexes.

Rute G Matos1, Ana Barbas, Cecília M Arraiano.   

Abstract

RNases are enzymes that process and degrade RNA molecules. As such, the study of the interactions between these enzymes and RNA molecules is essential in order to better understand their mechanism of action. In this report, our aim was to use E. coli RNase II as a model to compare two different techniques for the characterization and interpretation of the stability of RNA-protein complexes: Surface Plasmon Resonance and Electrophoretic Mobility Shift Assay.

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Year:  2010        PMID: 20589527     DOI: 10.1007/s10930-010-9265-1

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   2.371


  12 in total

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4.  Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex.

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5.  Determination of key residues for catalysis and RNA cleavage specificity: one mutation turns RNase II into a "SUPER-ENZYME".

Authors:  Ana Barbas; Rute G Matos; Mónica Amblar; Eduardo López-Viñas; Paulino Gomez-Puertas; Cecília M Arraiano
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Review 6.  The role of 3'-5' exoribonucleases in RNA degradation.

Authors:  José M Andrade; Vânia Pobre; Inês J Silva; Susana Domingues; Cecília M Arraiano
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7.  Characterizing ribonucleases in vitro examples of synergies between biochemical and structural analysis.

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Journal:  Methods Enzymol       Date:  2008       Impact factor: 1.600

8.  A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding.

Authors:  Mónica Amblar; Cecília M Arraiano
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Review 9.  Function, mechanism and regulation of bacterial ribonucleases.

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10.  New insights into the mechanism of RNA degradation by ribonuclease II: identification of the residue responsible for setting the RNase II end product.

Authors:  Ana Barbas; Rute G Matos; Mónica Amblar; Eduardo López-Viñas; Paulino Gomez-Puertas; Cecília M Arraiano
Journal:  J Biol Chem       Date:  2008-03-12       Impact factor: 5.157

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6.  The Molecular Basis of TnrA Control by Glutamine Synthetase in Bacillus subtilis.

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7.  An improved method for surface immobilisation of RNA: application to small non-coding RNA-mRNA pairing.

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