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On the recombinational origin of protein-sequence-subunit structure

E N Trifonov1

  • 1Institute of Molecular Medical Sciences, Palo Alto, CA 94306.

Journal of Molecular Evolution
|May 1, 1994
PubMed
Summary

Preferred protein sizes, around 125 amino acids (aa) for eukaryotes and 150 aa for prokaryotes, may stem from DNA circle recombination. This theory explains observed protein subunit sizes based on DNA helical repeats.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biophysics

Background:

  • The concept of preferred protein sizes has been observed since 1929.
  • Recent estimates suggest overrepresented protein sizes are multiples of 125 amino acids (aa) for eukaryotes and 150 aa for prokaryotes.

Purpose of the Study:

  • To propose and quantitatively develop a hypothesis explaining preferred protein sizes.
  • To investigate the recombinational nature of protein size regularity.

Main Methods:

  • Modeling protein evolution via DNA circle insertions.
  • Analyzing DNA circle contour lengths for divisibility by three and DNA helical repeat.
  • Calculating predicted protein subunit sizes based on DNA helical repeat values.

Main Results:

  • The model predicts optimal DNA circle lengths of 250-500 base pairs (bp).
  • These lengths correspond to preferred protein subunit sizes of 80-170 aa.
  • Calculated sizes of 125 aa and 150 aa are derived when DNA helical repeats are near 10.54 bp/turn.

Conclusions:

  • Recombinational events involving DNA circles of specific sizes likely drive preferred protein subunit sizes.
  • The DNA helical repeat significantly influences the resulting protein subunit size.
  • The hypothesis aligns with experimental observations of protein sizes and DNA properties.

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