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Literature summary for 3.1.26.3 extracted from

  • Leulliot, N.; Quevillon-Cheruel, S.; Graille, M.; van Tilbeurgh, H.; Leeper, T.C.; Godin, K.S.; Edwards, T.E.; Sigurdsson, S.T.; Rozenkrants, N.; Nagel, R.J.; Ares, M.; Varani, G.
    A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III (2004), EMBO J., 23, 2468-2477.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae the enzyme plays an important role in the maturation of a diverse set of RNAs ?
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q02555
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
double-stranded RNA + H2O the enzymatic activity requires a conserved catalytic domain, while RNA binding requires the double-stranded RNA-binding domain at the C-terminus of the protein. Rnt1p specifically cleaves RNAs that possess short irregular stem-loops containing 12–14 base pairs interrupted by internal loops and bulges and capped by conserved AGNN tetraloops. A new carboxy-terminal helix following a canonical ds double-stranded RNA-binding domain structure allows the Rnt1p double-stranded RNA-binding domain to bind to short RNA stem-loops by modulating the conformation of helix a1, a key RNA-recognition element of the double-stranded RNA-binding domain Saccharomyces cerevisiae 5'-phosphooligonucleotides
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additional information the enzyme plays an important role in the maturation of a diverse set of RNAs Saccharomyces cerevisiae ?
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?

Synonyms

Synonyms Comment Organism
RNase III
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Saccharomyces cerevisiae
RNT1
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Saccharomyces cerevisiae