EC Number   |
Protein Variants |
Reference  |
|---|
   3.1.13.1 | more |
hybrid proteins are constructed by replacing the S1 domain of RNase II for the S1 from RNase R and PNPase, and their exonucleolytic activity and RNA-binding ability are examined. Both the S1 domains of RNase R and PNPase are able to partially reverse the drop of RNA-binding ability and exonucleolytic activity resulting from removal of the S1 domain of RNase II. The S1 domains investigated are not equivalent |
677105 |
| 3.1.13.1 | more |
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 |
681386 |
| 3.1.13.1 | D551N |
mutation in Rrp44-cat abolishes the exonucleolytic activity of Rrp44 without affecting its ability to bind RNA |
681884 |
| 3.1.13.1 | D201N |
significant loss of activity in degradation of poly(A) (0.2% of that of the wild-type enzyme). Generates a 10-11-nt fragment as a major degradation product, although longer reaction times result in the usual 4-nt fragment as a secondary product |
693048 |
| 3.1.13.1 | D207N |
still retains 12% activity |
693048 |
| 3.1.13.1 | D210N |
significant loss of activity in degradation of poly(A) (0.3% of that of the wild-type enzyme). Generates a 10-11-nt fragment as a major degradation product, although longer reaction times result in the usual 4-nt fragment as a secondary product |
693048 |
| 3.1.13.1 | F358A |
the protein is 2fold more active than the wild-type |
693048 |
| 3.1.13.1 | Y253A |
26% of the activity of the enzyme persists, significantly impairs RNA binding |
693048 |
| 3.1.13.1 | Y253A/F358A |
12% of the activity of the enzyme persists, whereas RNA binding affinity is not significantly affected |
693048 |
| 3.1.13.1 | C425A |
cannot be classified as polymorphic in the Japanese population. In the Korean, Mongolian, Ovambo, Turkish, and German DNA no genotype other than homozygotic 425C allele in RNASE2 at each single nucleotide polymorphism site is found |
697158 |
