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NuMA/centrophilin: sequence analysis of the coiled-coil rod domain

D A Parry1

  • 1Department of Physics, Massey University, Palmerston North, New Zealand.

Biophysical Journal
|September 1, 1994
PubMed

Insights

Nuclear mitotic apparatus protein (NuMA) forms a parallel, two-stranded coiled-coil structure. Sequence analysis suggests this structure, while stabilized by ionic interactions, may not support filament aggregation in the nucleus.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Nuclear mitotic apparatus protein (NuMA), also known as centrophilin, possesses a central 1485-residue sequence.
  • This sequence exhibits a heptad substructure and a high propensity for alpha-helix formation.

Purpose of the Study:

  • To analyze the structural properties of the NuMA central coiled-coil domain.
  • To investigate the potential for NuMA aggregation into nuclear filaments based on sequence data.

Main Methods:

  • Bioinformatic analysis of the NuMA central sequence.
  • Identification of heptad substructure, coiled-coil formation propensity, and residue distribution patterns.

Main Results:

  • NuMA forms a two-stranded, parallel coiled-coil structure.
  • The coiled-coil conformation is interrupted by proline segments and phasing discontinuities.
  • Axial register is maintained and stabilized by numerous interchain ionic interactions.
  • The coiled-coil rod domain lacks long-range periodicity in acidic/basic residue distribution.

Conclusions:

  • The sequence data does not provide direct evidence for NuMA aggregation into closely packed filaments within the nucleus.
  • The structural characteristics suggest a stable coiled-coil rod but do not inherently promote filament formation.

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