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• W1708063932 endingPage "515" @default.
• W1708063932 startingPage "501" @default.
• W1708063932 abstract "RNase I, II, and IV are considered the most venerable of the known E. coli RNases. RNase I of E. coli was first discovered as a latent ribonuclease associated with ribosomes. RNase I is essentially a low-molecular-weight, basic protein with a single subunit. Denatured DNA inhibits RNase I activity by competitively binding to the enzyme. RNase digestion of all synthetic polynucleotide is stimulated by polyamines, although the degree of stimulation varies with substrate. Partial digestion of RNA by RNase I produces 2′, 3′-cyclic adenylic, cytidylic, guanylic, and uridylic phosphates as major acid-soluble products. When digestion is carried to completion, nucleoside 3′-monophosphates are generated. RNase II of E. coli was discovered as a K+-activated phosphodiesterase that was also ribosome-associated in extracts. The action of RNase II is highly dependent on RNA conformation with different optimal ionic conditions for different substrates. RNase IV of E. coli is not well recognized. It cleaves bacteriophage R17 RNA at limited sites and is generally useful in mapping genes along the RNA." @default.
• W1708063932 created "2016-06-24" @default.
• W1708063932 creator A5067725319 @default.
• W1708063932 creator A5079340049 @default.
• W1708063932 date "1982-01-01" @default.
• W1708063932 modified "2023-09-26" @default.
• W1708063932 title "16 RNases, I, II, and IV of Escherichia coli" @default.
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• W1708063932 doi "https://doi.org/10.1016/s1874-6047(08)60288-7" @default.
• W1708063932 hasPublicationYear "1982" @default.
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