The oligomerization of CynR in Escherichia coli | Academic Article individual record
abstract

Deletion analysis and alanine-scanning based on a homology-based interaction model were used to identify determinants of oligomerization in the transcriptional regulator CynR, a member of the LysR-type transcriptional regulator (LTTR) family. Deletion analysis confirmed that the putative regulatory domain of CynR was essential for driving the oligomerization of lambda repressor-CynR fusion proteins. The interaction surface of a different LTTR and OxyR was mapped onto a multiple sequence alignment of the LTTR family. This mapping identified putative contacts in the CynR regulatory domain dimer interface, which were targeted for alanine-scanning mutagenesis. Oligomerization was assayed by the ability of mutant lambda repressor-CynR fusions to assemble in E. coli revealing interesting similarities and differences between OxyR and CynR.

authors
author list (cited authors)
Knapp, G. S., & Hu, J. C.
publication date
2009
publisher
Wiley Publisher
published in
Protein Sci Journal
keywords
  • Lysr-type Transcriptional Regulators
  • Cynr
  • Oligomerization
  • Protein-protein Interactions
citation count

11