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Eukaryotic RNA Polymerases00:58

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RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Sequencing of mRNA from Whole Blood using Nanopore Sequencing
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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
Summary
This summary is machine-generated.

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.

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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.