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Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

M Kohlhoff1, A Dahm, R Hensel

  • 1FB 9 Mikrobiologie, Universität Essen, Germany.

FEBS Letters
|April 1, 1996
PubMed
Summary

Triosephosphate isomerase (TIM) from hyperthermophilic Archaea forms tetramers, unlike typical bacterial and eukaryotic dimers. This tetrameric structure correlates with thermoadaptation, not archaeal lineage, and the P. woesei TIM gene reveals the shortest sequence yet.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Extremophile Research

Background:

  • Triosephosphate isomerase (TIM) is a crucial enzyme in glycolysis.
  • Known TIM enzymes from bacteria and eukaryotes are typically dimers (48-60 kDa).
  • Hyperthermophilic organisms often exhibit unique protein structures adapted to extreme temperatures.

Purpose of the Study:

  • To characterize the structure and gene of Triosephosphate isomerase (TIM) from hyperthermophilic Archaea.
  • To investigate the correlation between TIM aggregation state and thermoadaptation.
  • To compare archaeal TIM with its bacterial and eukaryotic counterparts.

Main Methods:

  • Purification of TIM enzymes from Pyrococcus woesei and Methanothermus fervidus.
  • Molecular size determination using techniques like gel filtration or SDS-PAGE.

Related Experiment Videos

  • Cloning and sequencing of the TIM gene from P. woesei.
  • Sequence homology analysis and structural comparison.

    • Main Results:

    • TIM from hyperthermophilic Archaea (P. woesei, M. fervidus) exists as a homo-tetramer (100 kDa).
    • TIM from a mesophilic methanogen (Methanobacterium bryantii) is a dimer (57 kDa), suggesting tetramerization is linked to thermoadaptation.
    • The P. woesei TIM gene encodes the shortest known TIM sequence (224 residues), homologous to other TIMs.
    • Structural predictions suggest rearrangements in the archaeal TIM due to its shorter sequence, potentially forming new subunit contacts.

    Conclusions:

    • The tetrameric structure of TIM is an adaptation to thermophily, not an exclusive archaeal characteristic.
    • The shortest TIM sequence identified implies significant structural modifications for stability at high temperatures.
    • These findings contribute to understanding protein adaptation in hyperthermophilic archaea and enzyme evolution.