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Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate.
Lima WF, Wu H, Nichols JG, Prakash TP, Ravikumar V, Crooke ST. Lima WF, et al. Among authors: wu h. J Biol Chem. 2003 Dec 12;278(50):49860-7. doi: 10.1074/jbc.M306543200. Epub 2003 Sep 23. J Biol Chem. 2003. PMID: 14506260 Free article.
In a previous study, we showed that the RNA-binding domain of human RNase H1 is responsible for the positional preference for cleavage exhibited by the enzyme (Wu, H., Lima, W. F., and Crooke, S. T. (2001) J. Biol. Chem. 276, 23547-23553). Here, we identify the subs …
In a previous study, we showed that the RNA-binding domain of human RNase H1 is responsible for the positional preference for cleavage exhib …
Binding and cleavage specificities of human Argonaute2.
Lima WF, Wu H, Nichols JG, Sun H, Murray HM, Crooke ST. Lima WF, et al. Among authors: wu h. J Biol Chem. 2009 Sep 18;284(38):26017-28. doi: 10.1074/jbc.M109.010835. Epub 2009 Jul 22. J Biol Chem. 2009. PMID: 19625255 Free PMC article.
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