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• W1150082016 abstract "This chapter focuses on the enzymatic and chemical probing of ribosomal RNA–protein interactions. The protein-binding sites were first characterized partially by digesting complexes formed with in vivo32P-labeled RNA with ribonucleases. More recently, various enzymatic and chemical probes, in combination with rapid gel electrophoretic analyses, have been employed to examine these complexes at nucleotide level. Many protein-binding sites on ribosomal RNA have now been mapped by enzymatic and chemical methods. These approaches have suggested possible protein attachment sites, some of which have been investigated in greater detail by site-directed mutagenesis. Moreover, previously unidentified sites, such as those of E. coli proteins L2 and L3, have recently been characterized by synthesizing RNA domains using the T7 polymerase system, selectively binding the protein from total ribosomal proteins, and then probing the binding site. What is lacking now is more information on the conserved sequences and structure of the ribosomal proteins." @default.
• W1150082016 created "2016-06-24" @default.
• W1150082016 creator A5007322086 @default.
• W1150082016 creator A5058594816 @default.
• W1150082016 date "1988-01-01" @default.
• W1150082016 modified "2023-09-24" @default.
• W1150082016 title "[30] Enzymatic and chemical probing of ribosomal RNA—Protein interactions" @default.
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• W1150082016 doi "https://doi.org/10.1016/s0076-6879(88)64061-4" @default.
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