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Subunit interactions in Ascaris hemoglobin octamer formation

D M Minning1, A P Kloek, J Yang

  • 1Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri, USA.

The Journal of Biological Chemistry
|September 22, 1995
PubMed
Summary
This summary is machine-generated.

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The COOH-terminal tail is crucial but not solely responsible for Ascaris hemoglobin octamer formation. Other protein regions also contribute to the stability of this oxygen-avid hemoglobin structure.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Parasitology

Background:

  • Ascaris hemoglobin is an oxygen-avid homooctamer.
  • Each subunit possesses two homologous globin domains, with domain two (D2) featuring a COOH-terminal extension.

Purpose of the Study:

  • To investigate the role of the COOH-terminal extension in Ascaris hemoglobin multimer formation.
  • To identify other regions involved in stabilizing the octameric structure.

Main Methods:

  • Recombinant expression of globin domains (D1, D2) and modified proteins.
  • Chemical disruption of hemoglobin multimers using sodium thiocyanate (NaSCN).
  • Crystallographic analysis of domain interactions.

Main Results:

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  • The COOH-terminal tail alone is insufficient for multimerization when attached to myoglobin or D1.
  • Removal of the tail reduced, but did not abolish, multimerization of Ascaris hemoglobin and D2.
  • D2 dissociated more readily than full-length hemoglobin, suggesting D1 contributes to octamer stability.
  • Interactions at the D1 dimer interface involve hydrogen bonds, hydrophobic, and electrostatic forces.

    • Conclusions:

    • The COOH-terminal tail is necessary but not sufficient for efficient Ascaris hemoglobin octamer formation.
    • Other regions, including helices and loops within both globin domains, are critical for octamer stability.