Analysis of protein-RNA interactions in CRISPR proteins and effector complexes by UV-induced cross-linking and mass spectrometry

Methods

Volumn 89, Issue , 2015, Pages 138-148

  Sharma, Kundan ^a   Hrle, Ajla ^b   Kramer, Katharina ^a,h   Sachsenberg, Timo ^c   Staals, Raymond H J ^d   Randau, Lennart ^e   Marchfelder, Anita ^f   van der Oost, John ^d   Kohlbacher, Oliver ^c   Conti, Elena ^b   Urlaub, Henning ^a,g  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c UNIVERSITY OF TÜBINGEN   (Germany)

^d WAGENINGEN UNIVERSITY   (Netherlands)

^e MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

^f UNIVERSITY OF ULM   (Germany)

^g UNIVERSITY MEDICAL CENTER GÖTTINGEN   (Germany)

^h MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

Author keywords

Cas7; CRISPR Cas; Mass spectrometry; Protein RNA interactions; UV cross linking

Indexed keywords

ALCOHOL; CASPASE 7; CRISPR ASSOCIATED PROTEIN; OLIGONUCLEOTIDE; RECOMBINANT PROTEIN; RNA BINDING PROTEIN; PROTEIN BINDING; RNA;

ADAPTIVE IMMUNITY; ARTICLE; BINDING SITE; CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEAT; COMPLEX FORMATION; CONTROLLED STUDY; GEL MOBILITY SHIFT ASSAY; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN RNA BINDING; REVERSED PHASE LIQUID CHROMATOGRAPHY; RNA ANALYSIS; THERMOPROTEUS TENAX; THERMUS THERMOPHILUS; ULTRAVIOLET SPECTROSCOPY; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; METABOLISM; PHOTOSTIMULATION; PHYSIOLOGY; PROCEDURES; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TANDEM MASS SPECTROMETRY; ULTRAVIOLET RADIATION;

CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEATS; PHOTIC STIMULATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA; RNA-BINDING PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TANDEM MASS SPECTROMETRY; ULTRAVIOLET RAYS;

EID: 84946492121     PISSN: 10462023     EISSN: 10959130     Source Type: Journal    
DOI: 10.1016/j.ymeth.2015.06.005     Document Type: Article

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