Images

Figure 1. The secondary structure diagram of all three domains that make up the group I intron (4).


Figure 2. (a) A basic pathway for group I intron self-splicing. Step (1) is the first transesterification that takes place, resulting in a cleavage at the 5’-splice site. The intron goes through a conformation stage (Conf.) where the 3’-guanosine replaces the exogenous guanosine. The splicing comes to completion with the second transesterification step (2) with a cleavage at the 3’-spliesite and ligation of the two exons (5). (b) A basic pathway for group II intron self-splicing. In step (1) an internal adenosine acts as a nucleophile and attacks the 5’-splic site while forming a lariat-type structure. In step (2), the 3’ end of the 5’-exon cleaves the 3’-splice site, ligating the two exons and excising a lariat intron. 


Residues

Hydrogen Bond Partner

A-183

G-110

A-184

G-212, C-109

A-186

C-137, G-181, G-164

A-187

U-135

Table 1. Important hydrogen bonds between the adenosine residues in the A-rich bulge and the nucleotide residues in the P4 segment (6).

 

Residues

Hydrogen Bond Partner

A-151

U-224, A-248

A-152

U-224, C-223, G-250

A-153

C-223, G-250


Table 2.
Important hydrogen bonds between the adenosine residues in the tetraloop and the nucleotides in the tetraloop receptor region (6).

 

Residues

A-184

A-186

A-187

G-188

A-171

A-140

G-163

Table 3. Location of metal ligands in the P4-P6 domain (9).