Evidence of a conserved intrinsically disordered region in the C-terminus of the stringent response protein Rel from mycobacteria

FEBS Lett. 2014 May 2;588(9):1839-49. doi: 10.1016/j.febslet.2014.03.048. Epub 2014 Apr 6.

Abstract

The RelA/SpoT enzyme produces (p)ppGpp that helps the bacterium survive during stress. The domains present in it are interspersed with connecting linkers whose functions have been poorly elucidated. We rationally analyzed the sequence and structural property of the regulatory C-terminal region in the Rel family of proteins and report the presence of an intrinsically disordered region between two successive domains in this region that are separated by a defined amino acid sequence length. We show that the length and secondary structure of this linker are conserved in Rel proteins, further signifying its importance in rendering flexibility for domain movement and domain-domain interaction.

Keywords: Intrinsically disordered region; Mycobacteria; RelA/SpoT; Stringent response; ppGpp.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Circular Dichroism
  • Conserved Sequence
  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins
  • Ligases / chemistry*
  • Molecular Sequence Data
  • Mycobacterium smegmatis / enzymology*
  • Phylogeny
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Intrinsically Disordered Proteins
  • Ligases
  • guanosine 3',5'-polyphosphate synthetases