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RRNA small subunit pseudouridine methyltransferase Nep1

FieldValue
NameRRNA small subunit pseudouridine methyltransferase Nep1
EC_number2.1.1.260

RRNA small subunit pseudouridine methyltransferase Nep1 (, Nep1, nucleolar essential protein 1) is an enzyme with systematic name S-adenosyl-L-methionine:18S rRNA (pseudouridine1191-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

: S-adenosyl-L-methionine + pseudouridine1191 in yeast 18S rRNA \rightleftharpoons S-adenosyl-L-homocysteine + N1-methylpseudouridine1191 in yeast 18S rRNA

This enzyme recognizes specific pseudouridine residues (Psi) in small subunits of ribosomal RNA based on the local RNA structure.

A point mutation in the ribosome biogenesis factor Nep1 impairs its nucleolar localisation and RNA binding and causes the Bowen-Conradi syndrome. .

References

References

  1. (March 2008). "The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site". Nucleic Acids Research.
  2. (April 2010). "The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase". Nucleic Acids Research.
  3. (March 2011). "The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ1191 in yeast 18S rRNA". Nucleic Acids Research.
  4. (2011). "The Bowen-Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Psi 1191 in yeast 18S rRNA". Nucleic Acids Res.
  5. (2010). "The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase". Nucleic Acids Res.
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This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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