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Literature summary for 3.1.13.1 extracted from

  • Arraiano, C.M.; Barbas, A.; Amblar, M.
    Characterizing ribonucleases in vitro examples of synergies between biochemical and structural analysis (2008), Methods Enzymol., 447, 131-160.
    View publication on PubMed
Search for more literature for 3.1.13.1

Cloned(Commentary)

Cloned (Comment) Organism
RNase II wild-type, mutant and truncated proteins, cloned into plasmid pFCT6.1, overexpressed in Escherichia coli BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
native RNase II and its RNA-bound complex Escherichia coli

Protein Variants

Protein Variants Comment Organism
D209N has less than 1% of the wild-type RNase activity, has similar affinities for the RNA substrate as the wild-type enzyme Escherichia coli
additional information DELTACSDb and DELTAS1b mutants, are more than 90% soluble. Similarly, the solubility of the RNB derivative, which lacks both putative RNA-binding domains, is also greater than 90%. The DELTACSDa mutant is only 60% soluble. Elimination of the whole CSD domain (DELTACSDb) or part of it (DELTACSDa) does not affect the exonucleolytic activity of RNase II, and even improves its activity significantly Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information RNase II activity is blocked by the presence of double-stranded structures on the RNA molecule Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA ?
-
 ?
additional information Escherichia coli SK4803 RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli SK4803
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA Escherichia coli ?
-
 ?
additional information does not catalyze degradation of double-stranded RNA. RNase II has a CSD domain at the N-terminal end of the protein, a central RNB catalytic domain, and an S1 RNA-binding domain at the C-terminus. S1 domain is highly important for RNase II activity and its contribution to productive RNA binding is much more important than that of the CSD domain. This domain somehow prevents the rapid degradation of RNA by RNase II, which may be highly important to overall mRNA decay in Escherichia coli Escherichia coli ?
-
 ?
additional information RNase II is one of the major enzymes involved in mRNA processing. If the CSD is limiting the action of RNase II in vivo, it may play an important role working as a brake and thus preventing the massive degradation of RNA Escherichia coli SK4803 ?
-
 ?
additional information does not catalyze degradation of double-stranded RNA. RNase II has a CSD domain at the N-terminal end of the protein, a central RNB catalytic domain, and an S1 RNA-binding domain at the C-terminus. S1 domain is highly important for RNase II activity and its contribution to productive RNA binding is much more important than that of the CSD domain. This domain somehow prevents the rapid degradation of RNA by RNase II, which may be highly important to overall mRNA decay in Escherichia coli Escherichia coli SK4803 ?
-
 ?
mRNA + H2O synthetic mRNA substrates, either with or without a poly(A) tail, turn out to be a good choice for mimicking the actual in vivo enzyme substrates Escherichia coli 5'-phosphomononucleotides
-
 ?
mRNA + H2O synthetic mRNA substrates, either with or without a poly(A) tail, turn out to be a good choice for mimicking the actual in vivo enzyme substrates Escherichia coli SK4803 5'-phosphomononucleotides
-
 ?
poly(A) + H2O RNase II has a strong preference for poly(A) stretches and is highly efficient in degrading poly(A) tails. RNase II is responsible for 90% of the exonucleolytic degradation of synthetic RNA poly(A) homopolymers Escherichia coli 5'-AMP + oligo(A)
-
 ?
poly(A) + H2O RNase II has a strong preference for poly(A) stretches and is highly efficient in degrading poly(A) tails. RNase II is responsible for 90% of the exonucleolytic degradation of synthetic RNA poly(A) homopolymers Escherichia coli SK4803 5'-AMP + oligo(A)
-
 ?
ssRNA + H2O
-
 Escherichia coli ?
-
 ?
ssRNA + H2O
-
 Escherichia coli SK4803 ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase II
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Escherichia coli