The role of semidisorder in temperature adaptation of bacterial FlgM proteins

Biophys J. 2013 Dec 3;105(11):2598-605. doi: 10.1016/j.bpj.2013.10.026.

Abstract

Probabilities of disorder for FlgM proteins of 39 species whose optimal growth temperature ranges from 273 K (0°C) to 368 K (95°C) were predicted by a newly developed method called Sequence-based Prediction with Integrated NEural networks for Disorder (SPINE-D). We showed that the temperature-dependent behavior of FlgM proteins could be separated into two subgroups according to their sequence lengths. Only shorter sequences evolved to adapt to high temperatures (>318 K or 45°C). Their ability to adapt to high temperatures was achieved through a transition from a fully disordered state with little secondary structure to a semidisordered state with high predicted helical probability at the N-terminal region. The predicted results are consistent with available experimental data. An analysis of all orthologous protein families in 39 species suggests that such a transition from a fully disordered state to semidisordered and/or ordered states is one of the strategies employed by nature for adaptation to high temperatures.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Algorithms
  • Amino Acid Sequence
  • Bacteria / chemistry
  • Bacteria / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Hot Temperature*
  • Molecular Dynamics Simulation*
  • Molecular Sequence Data
  • Protein Conformation
  • Species Specificity

Substances

  • Bacterial Proteins
  • FlgM protein, Bacteria