Literature DB >> 18982294

Structural analysis of protein-RNA interactions with mass spectrometry.

Mamuka Kvaratskhelia1, Stuart F J Le Grice.   

Abstract

We present a high-resolution mass spectrometric footprinting approach enabling the identification of amino acids in the protein of interest interacting with cognate RNA. This approach is particularly attractive for studying large nucleoprotein complexes that are less amenable to crystallographic or nuclear magnetic resonance analysis. Importantly, our methodology allows examination of protein-RNA interactions under biologically relevant conditions using limited amounts of protein and nucleic acid samples.

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Year:  2008        PMID: 18982294      PMCID: PMC2586912          DOI: 10.1007/978-1-60327-475-3_15

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  10 in total

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4.  Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent.

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5.  Structural basis of m7GpppG binding to the nuclear cap-binding protein complex.

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9.  Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain.

Authors:  Jin-Biao Ma; Keqiong Ye; Dinshaw J Patel
Journal:  Nature       Date:  2004-05-20       Impact factor: 49.962

10.  The X-ray structure of Escherichia coli RraA (MenG), A protein inhibitor of RNA processing.

Authors:  Arthur F Monzingo; Junjun Gao; Ji Qiu; George Georgiou; Jon D Robertus
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  10 in total
  7 in total

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2.  Use of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzyme.

Authors:  Tien-Hao Chen; Akiko Tanimoto; Nikoloz Shkriabai; Mamuka Kvaratskhelia; Vicki Wysocki; Venkat Gopalan
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3.  HIV-1 Integrase Binds the Viral RNA Genome and Is Essential during Virion Morphogenesis.

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Review 7.  Next-generation sequencing: A new avenue to understand viral RNA-protein interactions.

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  7 in total

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