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Literature summary for 2.1.1.216 extracted from

  • Edqvist, J.; Grosjean, H.; Straby, K.B.
    Identity elements for N2-dimethylation of guanosine-26 in yeast tRNAs (1992), Nucleic Acids Res., 20, 6575-6581.
    View publication on PubMedView publication on EuropePMC

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in yeast tRNAAsp G26 is unmodified. Successive change of the near surroundings of G26 in this tRNA is performed until G26 becomes modified to N2-dimethylguanine26 tRNA by a tRNA(m2(2)G26)methyltransferase in Xenopus laevis oocytes. In this the two D-stem basepairs C1 -G24, G10-C25 are identified immediately preceding G26 as major identity elements for the dimethylating enzyme modifying G26. Increasing the extra loop in tRNAAsp from four to the more usual five bases influence the global structure of the tRNA such that the mJG26 formation is drastically decreased even if the near region of G26 had the two consensus basepairs. Not only are the two consensus base pairs in the D-stem a prerequisite for G26 modification, but also is any part of the tRNA molecule that influence the 3D-structure important for the recognition between nuclear coded tRNAs and the tRNA(mJG26)methyltransferase Saccharomyces cerevisiae ?
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