NDLI: Chemical modification interference.

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Chemical modification interference.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nilsen, Timothy W.
Abstract	Chemical modification interference is a powerful method for surveying an entire RNA molecule to identify functionally important chemical groups. The basic idea is to generate a pool of end-labeled RNAs wherein each RNA molecule is chemically modified (e.g., by diethyl pyrocarbonate [DEPC], hydrazine, dimethyl sulfate, CMCT, or kethoxal) at a different position. The pool of RNAs is then allowed to participate in the reaction of interest. The functionally important RNA molecules (e.g., those bound by protein or that successfully participate in a processing reaction) are then separated from the nonfunctional RNA molecules (e.g., those not bound by protein or unable to participate in a processing reaction). This is often achieved by straightforward gel electrophoretic analysis. In the case of protein binding, it is necessary to be able to separate bound RNA from unbound RNA, which can be accomplished using electrophoretic mobility shift assays, filter binding, or affinity approaches (e.g., by immunoprecipitation or the use of tagged proteins). None of these techniques requires that a large fraction of RNA be bound or reacted, and, as a result, they are quite sensitive. Here we describe one example of a chemical modification interference assay in which RNA is modified with DEPC or hydrazine before binding to a protein. This technique can be readily adapted for use with other chemicals.
File Format	HTM / HTML
ISSN	19403402
Issue Number	6
Volume Number	2015
e-ISSN	15596095
Journal	Cold Spring Harbor Protocols
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2015-06-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Clinical Laboratory Techniques Binding Sites Drug Effects Diethyl Pyrocarbonate Pharmacology Hydrazines Nucleic Acid Conformation Rna Adenosine Physiology Guanosine Protein Binding Isolation & Purification Uridine Journal Article
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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