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Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA

Hasan Demirci1, Steven T Gregory, Albert E Dahlberg

  • 1Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI, USA.

The EMBO Journal
|January 12, 2007
PubMed

Insights

The bacterial methyltransferase PrmA trimethylates ribosomal protein L11. Structural studies reveal how PrmA binds L11 and its cofactor S-adenosyl-L-methionine to catalyze multiple methylation reactions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Bacterial ribosomal protein L11 undergoes post-translational trimethylation.
  • This modification is catalyzed by the methyltransferase PrmA.
  • PrmA modifies multiple residues on L11.

Purpose of the Study:

  • To elucidate the structural basis of PrmA activity.
  • To understand the mechanism of L11 trimethylation by PrmA.
  • To investigate PrmA interaction with its substrate and cofactor.

Main Methods:

  • X-ray crystallography
  • Determination of apo-PrmA structures
  • Determination of PrmA-cofactor complex structure
  • Determination of PrmA-L11 enzyme-substrate complex structure

Main Results:

  • Four distinct structures of PrmA from Thermus thermophilus were determined.
  • Structures revealed domain flexibility enabling sequential methylation of L11.
  • The enzyme-substrate complex structure highlighted specific L11 N-terminal domain interaction and Lys39 positioning.
  • A unique flexible loop suggests efficient cofactor/product exchange.

Conclusions:

  • PrmA's domain arrangement facilitates multiple methylations on L11.
  • Specific interactions explain PrmA's preference for L11 prior to ribosomal assembly.
  • Structural insights provide a mechanistic understanding of bacterial ribosomal protein modification.

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