Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a large set of RNase II truncated proteins and comparison of them to the wild-type regarding their exoribonucleolytic activity and RNA-binding ability. The dissociation constants are determined using different single- or double-stranded substrates. The results obtained reveal that S1 is the most important domain in the establishment of stable RNAprotein complexes, and its elimination results in a drastic reduction on RNA-binding ability. The N-terminal CSD plays a very specific role in RNase II, preventing a tight binding of the enzyme to single-stranded poly(A) chains. The biochemical results obtained with a mutant that lacks both putative RNA-binding domains, reveals the presence of an additional region involved in RNA binding. Such region, is identified by sequence analysis and secondary structure prediction as a third putative RNA-binding domain located at the N-terminal part of RNB catalytic domain | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
oligonucleotide + H2O | - |
Escherichia coli | ? | - |
? | |
poly(A) + H2O | - |
Escherichia coli | ? | - |
? |