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Literature summary extracted from

  • Torchia, C.; Takagi, Y.; Ho, C.K.
    Archaeal RNA ligase is a homodimeric protein that catalyzes intramolecular ligation of single-stranded RNA and DNA (2008), Nucleic Acids Res., 36, 6218-6227.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.5.1.3 expression in Escherichia coli Methanothermobacter thermautotrophicus

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.3 additional information expression of N-terminal amino acids 1-253 gives a protein defective in overall ligation but retaining the ability to form EpA intermediate, bind to pRNA and transfer AMP to pRNA, albeit less efficiently than wild-type ligase. Expression of amino acids 255-381 results in a protein that fails to form a detectable protein-RNA complex and does not support overall ligation or RNA circularization Methanothermobacter thermautotrophicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.5.1.3 45000
-
 2 * 45000, calculated and sedimentation analysis Methanothermobacter thermautotrophicus

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.3 Methanothermobacter thermautotrophicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.3 (deoxyribonucleotide)n
-
 Methanothermobacter thermautotrophicus circular (deoxyribonucleotide)n
-
 ?
6.5.1.3 (ribonucleotide)n
-
 Methanothermobacter thermautotrophicus circular (ribonucleotide)n
-
 ?
6.5.1.3 ATP + (deoxyribonucleotide)n
-
 Methanothermobacter thermautotrophicus adenylyl-(deoxyribonucleotide)n + diphosphate
-
 ?
6.5.1.3 ATP + (ribonucleotide)n
-
 Methanothermobacter thermautotrophicus adenylyl-(ribonucleotide)n + diphosphate
-
 ?
6.5.1.3 additional information enzyme does not discriminate between RNA and DNA for phosphodiester bond formation Methanothermobacter thermautotrophicus ?
-
 ?
6.5.1.3 additional information intramolecular ligation of 5'-PO4 single-strand RNA to form a covalently closed circular RNA molecule through ligase-adenylylate and RNA-adenylylate intermediates AppRNA. At the optimal temperature of 65°C, AppRNA is predominantly ligated to a circular product. At 35°C, phosphodiester bond formation is suppressed and the majority of the AppRNA is deadenylylated Methanothermobacter thermautotrophicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.5.1.3 dimer 2 * 45000, calculated and sedimentation analysis Methanothermobacter thermautotrophicus
6.5.1.3 More the C-terminal 127 amino acid segment is required for dimerization Methanothermobacter thermautotrophicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.5.1.3 65
-
 RNA-adenylylate intermediates AppRNA are predominantly ligated to a circular product Methanothermobacter thermautotrophicus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
6.5.1.3 35
-
 phosphodiester bond formation is suppressed and the majority of the RNA-adenylylate intermediates AppRNA are deadenylylated Methanothermobacter thermautotrophicus