Erratum to “Asymmetric Allosteric Activation of the Symmetric ArgR Hexamer” [J. Mol. Biol. (2005) 346, 43–56]

Jin, Lihua; Xue, Wei‐Feng; Fukayama, June Wong; Yetter, Jaclyn; Pickering, Michael D.; Carey, Jannette

doi:10.1016/j.jmb.2005.01.056

Cited by 3 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Isothermal titration calorimetry, surface plasmon resonance and proteolysis experiments with E. coli ArgR have shown that all six l-arginine-binding sites have equal intrinsic affinities for their ligand; however, occupancy of a single site causes a conformation change which resets the remaining five sites, making them 100-fold weaker (Jin et al, 2004). However, in the crystal structures of E. coli apo-and holo-ArgR C-terminal domain hexamers no net reorientation of the trimers was observed (Van Duyne et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

Structure of the C-terminal effector-binding domain of AhrC bound to its corepressorL-arginine

et al. 2007

View full text Add to dashboard Cite

The arginine repressor/activator protein (AhrC) from Bacillus subtilis belongs to a large family of multifunctional transcription factors that are involved in the regulation of bacterial arginine metabolism. AhrC interacts with operator sites in the promoters of arginine biosynthetic and catabolic operons, acting as a transcriptional repressor at biosynthetic sites and an activator of transcription at catabolic sites. AhrC is a hexamer of identical subunits, each having two domains. The C-terminal domains form the core of the protein and are involved in oligomerization and L-arginine binding. The N-terminal domains lie on the outside of the compact core and play a role in binding to 18 bp DNA operators called ARG boxes. The C-terminal domain of AhrC has been expressed, purified and characterized, and also crystallized as a hexamer with the bound corepressor L-arginine. Here, the crystal structure refined to 1.95 A is presented.

show abstract

Section: Discussionmentioning

confidence: 99%

Structure of the C-terminal effector-binding domain of AhrC bound to its corepressorL-arginine

et al. 2007

View full text Add to dashboard Cite

show abstract

“…In the NAhrC structure, Gln22 forms a network of hydrogen bonds with Gln38 and Ser42 and it has been suggested that this will make up the specific repressor-DNA interface (Ni et al, 1999). It is anticipated that upon binding of the co-repressor l-arginine and the subsequent conformational change within the C-terminal domains (Van Duyne et al, 1996;Ni et al, 1999;Jin et al, 2004), the DNA-binding domains will come closer together allowing them to form dimers, where each monomer will then be able to occupy one half site of the ARG box. The 1 sheet is almost exclusively hydrophobic and is a good candidate for the dimer interface.…”

Section: Discussionmentioning

confidence: 99%

A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein fromBacillus subtilis

et al. 2007

View full text Add to dashboard Cite

In Bacillus subtilis the concentration of L-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor L-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 A resolution is presented.

show abstract

“…Unlike other bacterial repressors, which are usually physiologically active as dimers, trimers or tetramers, ArgR binds to DNA in a hexameric form, corresponding to a molecular weight (MW) of ∼100 kDa 1–5 . L ‐Arginine binds to ArgR and increases its affinity and specificity for DNA operator sequences by allosteric activation 6. ArgR also plays an important role in ColE1 plasmid site‐specific recombination, a process that converts plasmid multimers into monomers during replication and is required for stable plasmid inheritance 7.…”

mentioning

confidence: 99%

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

Šamalíková

Carey

Grandori

2005

Rapid Comm Mass Spectrometry

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Erratum to “Asymmetric Allosteric Activation of the Symmetric ArgR Hexamer” [J. Mol. Biol. (2005) 346, 43–56]

Cited by 3 publications

References 0 publications

Structure of the C-terminal effector-binding domain of AhrC bound to its corepressorL-arginine

Structure of the C-terminal effector-binding domain of AhrC bound to its corepressorL-arginine

A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein fromBacillus subtilis

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

Contact Info

Product

Resources

About