PMID:16106344
| Citation |
Samalíková, M, Carey, J and Grandori, R (2005) Assembly of the hexameric Escherichia coli arginine repressor investigated by nano-electrospray ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 19:2549-52 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1002/rcm.2094 |
| Keywords |
Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Gene Expression; Protein Structure, Quaternary; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Spectrometry, Mass, Electrospray Ionization/methods |
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