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Literature summary extracted from

  • Dorleans, A.; Li de la Sierra-Gallay, I.; Piton, J.; Zig, L.; Gilet, L.; Putzer, H.; Condon, C.
    Molecular basis for the recognition and cleavage of RNA by the bifunctional 5'-3' exo/endoribonuclease RNase J (2011), Structure, 19, 1252-1261.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.22 enzyme with bound 4 nt RNA with sequence CUGG or a 16 nt RNA, using catalytically inactive mutant H77A and a 2'-O-methylated, 3'-fluorescein-labeled RNAs, X-ray diffraction crystal structure determination and analysis at 2.5-3.1 A resolution, molecular replacement Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.22 H77A catalytically inactive mutant Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.22 Zn2+ binding structure in the beta-lactamase domain of the enzyme, overview Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.6.1.22 additional information Bacillus subtilis RNase J is a bifunctional 5'-3' exo/endoribonuclease ?
-
 ?
4.6.1.22 additional information Thermus thermophilus RNase J is a bifunctional 5'-3' exo/endoribonuclease, structure of enzyme bound to a 4-nucleotide RNA showing an RNA-binding channel. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.22 Bacillus subtilis
-
-
-
4.6.1.22 Thermus thermophilus Q72JJ7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.22 additional information RNase J is a bifunctional 5'-3' exo/endoribonuclease Bacillus subtilis ?
-
 ?
4.6.1.22 additional information RNase J is a bifunctional 5'-3' exo/endoribonuclease, structure of enzyme bound to a 4-nucleotide RNA showing an RNA-binding channel. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode Thermus thermophilus ?
-
 ?
4.6.1.22 additional information the enzyme RNase J1 shows processive behavior on long RNAs, and behaves distributively for substrates less than 5 nucleotides in length, RNA substrate binding structure and mechansim of the enzyme, overview Bacillus subtilis ?
-
 ?
4.6.1.22 additional information the enzyme RNase J1 shows processive behavior on long RNAs, and behaves distributively for substrates less than 5 nucleotides in length, RNA substrate binding structure and mechansim of the enzyme, overview Thermus thermophilus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.6.1.22 bifunctional 5'-3' exo/endoribonuclease
-
 Bacillus subtilis
4.6.1.22 bifunctional 5'-3' exo/endoribonuclease
-
 Thermus thermophilus
4.6.1.22 RNase J
-
 Bacillus subtilis
4.6.1.22 RNase J
-
 Thermus thermophilus
4.6.1.22 RNase J1
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
4.6.1.22 evolution RNase J is a key member of the beta-CASP family of metallo-beta-lactamases Bacillus subtilis
4.6.1.22 evolution RNase J is a key member of the beta-CASP family of metallo-beta-lactamases Thermus thermophilus
4.6.1.22 additional information modeling of the enzyme reaction involving the binding of the RNA to the surface of the beta-CASP domain to explain the enzyme's processive action, enzyme residues involved in RNA recognition, overview. RNA-binding channel and proposed nucleotide exit tunnel of RNase J, model of Bacillus subtilis RNase J1/J2 heterodimer bound to RNA, overview Bacillus subtilis
4.6.1.22 additional information modeling of the enzyme reaction involving the binding of the RNA to the surface of the beta-CASP domain to explain the enzyme's processive action, enzyme residues involved in RNA recognition, RNA-binding channel and proposed nucleotide Exit tunnel of RNase J, modeling, overview Thermus thermophilus
4.6.1.22 physiological function enzyme RNase J has been shown to play an extensive role in mRNA turnover. The bifunctional 5'-3' exo/endoribonuclease RNase J is involved in the maturation and turnover of RNAs in prokaryotes Bacillus subtilis
4.6.1.22 physiological function enzyme RNase J has been shown to play an extensive role in mRNA turnover. The bifunctional 5'-3' exo/endoribonuclease RNase J is involved in the maturation and turnover of RNAs in prokaryotes Thermus thermophilus