Interdomain linkers of homologous response regulators determine their mechanism of action

Don Walthers, Van K. Tran, Linda Kenney

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

OmpR and PhoB are response regulators that contain an N-terminal phosphorylation domain and a C-terminal DNA binding effector domain connected by a flexible interdomain linker. Phosphorylation of the N terminus results in an increase in affinity for specific DNA and the subsequent regulation of gene expression. Despite their sequence and structural similarity, OmpR and PhoB employ different mechanisms to regulate their effector domains. Phosphorylation of OmpR in the N terminus stimulates the DNA binding affinity of the C terminus, whereas phosphorylation of the PhoB N terminus relieves inhibition of the C terminus, enabling it to bind to DNA. Chimeras between OmpR and PhoB containing either interdomain linker were constructed to explore the basis of the differences in their activation mechanisms. Our results indicate that effector domain regulation by either N terminus requires its cognate interdomain linker. In addition, our findings suggest that the isolated C terminus of OmpR is not sufficient for a productive interaction with RNA polymerase.

Original languageEnglish (US)
Pages (from-to)317-324
Number of pages8
JournalJournal of Bacteriology
Volume185
Issue number1
DOIs
StatePublished - Jan 1 2003
Externally publishedYes

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Phosphorylation
DNA
Gene Expression Regulation
DNA-Directed RNA Polymerases

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Interdomain linkers of homologous response regulators determine their mechanism of action. / Walthers, Don; Tran, Van K.; Kenney, Linda.

In: Journal of Bacteriology, Vol. 185, No. 1, 01.01.2003, p. 317-324.

Research output: Contribution to journalArticle

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