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A sequence motif in many polymerases

P Argos1

  • 1European Molecular Biology Laboratory, Heidelberg, FRG.

Nucleic Acids Research
|November 11, 1988
PubMed

Insights

A conserved 15-residue sequence motif in polymerases, featuring a Tyr-Gly-Asp-(Thr)-Asp core, is identified. This motif may play a crucial role in enzyme catalysis and magnesium binding, impacting DNA and RNA synthesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Polymerases are crucial enzymes involved in DNA and RNA synthesis across various species.
  • Sequence analysis has revealed conserved regions within enzymes, suggesting functional importance.

Purpose of the Study:

  • To identify and characterize a conserved sequence motif in polymerases.
  • To investigate the potential functional significance of this motif in enzyme activity.

Main Methods:

  • Sequence analysis of diverse polymerases.
  • Identification of a 15-residue conserved motif.

Main Results:

  • A conserved 15-residue motif, including a Tyr-Gly-Asp-(Thr)-Asp core and flanking hydrophobic regions, was identified in various polymerases.
  • The motif was also suggested to be present in mRNA maturase segments.
  • The aspartate residues within the motif are hypothesized to be critical for polymerase function, potentially through catalysis or magnesium ion binding.

Conclusions:

  • A novel conserved sequence motif in polymerases has been discovered.
  • This motif is likely essential for polymerase function, possibly mediating catalysis and/or magnesium binding.
  • The findings provide insights into the molecular mechanisms of DNA and RNA synthesis.

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