Structure of the Hairpin

Ribozyme

Nate Steele
Ribozymes:
In biological molecules there are two types of catalysts: proteins (which everyone
knows about) and the lesser known RNA catalysts called ribozymes. When Tom Cech
first proposed the idea of ribozymes while working on Tetrahymena thermophila it
was like saying the earth was round in Columbus' day. The idea that RNA could act as
a catalyst was truly unheard of. The question then arises of what exactly do ribozymes
do? These ribozymes are self splicing and many of these, like the Hammerhead, cut
out there own intron using nucleophilic attack and transesterification reactions. I like
to call them suicide bombers.

The Hairpin Ribozyme
The hairpin ribozyme consists of a family of small ribozymes found in certain plant
viruses. The crystal structure that we will look at is from the satellite RNA of the
Tobacco Ring spot virus. It is responsible for the self-catalytic cleavage and the
rejoining of circles of single copies of satellite RNA during its rolling cycle
replication. (Recall that in rolling cycle replication RNA is spliced, unwound, and
replicated in a circle). Being that proteins posses so many different amino acids, with
many different properties, it comes as no surprise that they can activate and cleave
with high specificity. With RNA there are only four bases, which results in less room
to work with. For this simple reason, most ribozymes possess metal ions in there
active site. What makes the Hairpin Ribozyme remarkable is that it contains no metals
in its active site. The catalysis is done completely with RNA bases acting in a similar
fashion to acid base cleavage.