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Literature summary for 6.5.1.3 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
Search for more literature for 6.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanothermobacter thermautotrophicus

Protein Variants

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(deoxyribonucleotide)n
-
 Methanothermobacter thermautotrophicus circular (deoxyribonucleotide)n
-
 ?
(ribonucleotide)n
-
 Methanothermobacter thermautotrophicus circular (ribonucleotide)n
-
 ?
ATP + (deoxyribonucleotide)n
-
 Methanothermobacter thermautotrophicus adenylyl-(deoxyribonucleotide)n + diphosphate
-
 ?
ATP + (ribonucleotide)n
-
 Methanothermobacter thermautotrophicus adenylyl-(ribonucleotide)n + diphosphate
-
 ?
additional information enzyme does not discriminate between RNA and DNA for phosphodiester bond formation Methanothermobacter thermautotrophicus ?
-
 ?
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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