Assembly of the hexameric Escherichia coli arginine repressor investigated by nano-electrospray ionization time-of-flight mass spectrometry

Mária Šamalíková, Jannette Carey, Rita Grandori

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The arginine repressor (ArgR) from Escherichia coli regulates genes for L-arginine metabolism and is a required recombination factor for colE1 plasmid replication. Both functions require binding of L-arginine to the protein. In this work, nano-electrospray ionization time-of-flight mass spectrometry (nano-ESI-TOFMS) is used to study conformational and oligomeric states of intact ArgR and its isolated structural domains. In agreement with X-ray diffraction studies, it is shown that ArgR oligomerizes to form hexamers in both the presence and absence of L-arginine, and the basic unit of oligomerization appears to be the trimer. Higher-order assembly into dodecamers is also detected. The isolated C-terminal domain is found to associate into trimers and hexamers whereas the N-terminal domain is detected in its monomeric form. The observed species distributions suggest a role for the N-terminal domain in hexamer stabilization.

Original languageEnglish (US)
Pages (from-to)2549-2552
Number of pages4
JournalRapid Communications in Mass Spectrometry
Volume19
Issue number18
DOIs
StatePublished - Sep 29 2005

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Spectroscopy
  • Organic Chemistry

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