The antitermination activity of bacteriophage lambda N protein is controlled by the kinetics of an RNA-looping-facilitated interaction with the transcription complex |
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Authors: | Conant Clarke R Goodarzi Jim P Weitzel Steven E von Hippel Peter H |
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Affiliation: | Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA |
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Abstract: | |
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Keywords: | RNAP, RNA polymerase RNase, ribonuclease dsDNA, double-stranded DNA ssDNA, single-stranded DNA NTP, nucleoside triphosphates EDTA, ethylenediaminetetraacetic acid CTP, cytidine 5&prime -triphosphate GTP, guanosine 5&prime -triphosphate ApU, adenylyl-3&prime ,5&prime -uridine polyr (U), polyuridylic acid |
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