FlgM proteins from different bacteria exhibit different structural characteristics

Wai Kit Ma, Rachel Hendrix, Claire Stewart, Eric V. Campbell, Mitchell Lavarias, Kolyn Morris, Shauna Nichol, Matthew J Gage

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Intrinsically disordered proteins (IDPs) are a unique class of proteins that do not require a stable structure for function. The importance of IDPs in many biological processes has been established but there remain unanswered questions about their evolution and conservation of their disordered state within a protein family. Our group has been studying the structural similarities among orthologous FlgM proteins, a model class of IDPs. We have previously shown that the FlgM protein from the thermophile Aquifex aeolicus has more structure at A. aeolicus' physiological temperature (85 C) than is observed for the Salmonella typhimurium FlgM, suggesting that the disordered nature of FlgM varies among organisms and is not universally conserved. In this work, we extend these studies to the FlgM proteins from Escherichia coli, Pseudomonas aeruginosa, Proteus mirabilis, and Bacillus subtilis. We demonstrate that the B. subtilis, E. coli, and S. typhimurium FlgMs exist in a premolten globule-like conformation, though the B. subtilis FlgM is in a more compacted conformation than the other two. The P. aeruginosa and P. mirabilis FlgM proteins exist in a currently unknown conformation that is not either coil-like or premolten globule-like. The P. aeruginosa FlgM appears to contain more weak intramolecular contacts given its more compacted state than the P. mirabilis FlgM. These results provide experimental evidence that members of the same protein family can exhibit different degrees of disorder, though understanding how different disordered states evolve in the same protein family will require more study.

Original languageEnglish (US)
Pages (from-to)808-816
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1834
Issue number4
DOIs
StatePublished - Apr 2013

Fingerprint

Intrinsically Disordered Proteins
Proteus mirabilis
Bacillus subtilis
Proteins
Pseudomonas aeruginosa
Conformations
Salmonella typhimurium
Biological Phenomena
Salmonella
Escherichia coli Proteins
Bacilli
Bacteria FlgM protein
Escherichia coli
Conservation
Temperature

Keywords

  • Circular dichroism
  • FlgM
  • Intrinsically disordered protein
  • Molten globule

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

FlgM proteins from different bacteria exhibit different structural characteristics. / Ma, Wai Kit; Hendrix, Rachel; Stewart, Claire; Campbell, Eric V.; Lavarias, Mitchell; Morris, Kolyn; Nichol, Shauna; Gage, Matthew J.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1834, No. 4, 04.2013, p. 808-816.

Research output: Contribution to journalArticle

Ma, Wai Kit ; Hendrix, Rachel ; Stewart, Claire ; Campbell, Eric V. ; Lavarias, Mitchell ; Morris, Kolyn ; Nichol, Shauna ; Gage, Matthew J. / FlgM proteins from different bacteria exhibit different structural characteristics. In: Biochimica et Biophysica Acta - Proteins and Proteomics. 2013 ; Vol. 1834, No. 4. pp. 808-816.
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