Why ribozyme interacts with phosphate oxygen atom at cleavage site?
Answers
Explanation:
Evidence from the use of a phosphorothioate substrate analog suggests that the ribozyme interacts with one of the two nonbridging phosphate oxygen atoms at the cleavage site, but not via inner-sphere coordination with a divalent metal ion at the active site.
Answer:
Self-cleaving ribozymes are widespread across all domains of life and their architectural diversity is unmatched by any other type of natural catalytic RNA. These ribozymes have the ability to cleave their ribose-phosphate backbone at specific sites via internal phosphoester transfer with rate constants that typically exceed 10 million fold over that of spontaneous RNA degradation. The nine known self-cleaving ribozyme classes are able to accomplish this function by using a variety of structures that form unique catalytic cores (Doherty and Doudna 2000; Ferré-D'Amaré and Scott 2010; Eiler et al. 2014; Liu et al. 2014; Ren et al. 2014).