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Transcription
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PDB id
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3f3x
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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intracellular
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1 term
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Biological process
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regulation of transcription
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3 terms
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Biochemical function
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DNA binding
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2 terms
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DOI no:
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J Mol Biol
388:559-569
(2009)
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PubMed id:
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Structural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in archaea by MarR family proteins.
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A.Di Fiore,
G.Fiorentino,
R.M.Vitale,
R.Ronca,
P.Amodeo,
C.Pedone,
S.Bartolucci,
G.De Simone.
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ABSTRACT
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The multiple antibiotic resistance regulator (MarR) family constitutes a
significant class of transcriptional regulators whose members control a variety
of important biological functions such as regulation of response to
environmental stress, control of virulence factor production, resistance to
antimicrobial agents, and regulation of aromatic catabolic pathways. Although
the majority of MarR family members have been characterized as transcriptional
repressors, a few examples of transcriptional activators have also been
reported. BldR is a newly identified member of this family that has been
demonstrated to act as a transcriptional activator in stress response to
aromatic compounds in the crenarchaeon Sulfolobus solfataricus. In this work, we
report findings on the BldR X-ray crystal structure and present a molecular
modeling study on the complex that this protein forms with its cognate DNA
sequence, thus providing the first detailed description of the DNA-binding
mechanism of an archaeal activator belonging to the MarR family. Two residues
responsible for the high binding specificity of this transcriptional regulator
were also identified. Our studies demonstrated that, in Archaea, the capability
of MarR family members to act as activators or repressors is not related to a
particular DNA-binding mechanism but rather could be due to the position of the
binding site on the target DNA. Moreover, since genes encoding MarR proteins
often control transcription of operons that encode for multisubstrate efflux
pumps, our results also provided important insights for the identification of
new tools to overcome the microorganism's multidrug resistance.
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Selected figure(s)
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Figure 1.
Fig. 1. Ribbon representation of the BldR monomer with the
elements of secondary structure labeled (α1, 2–34; α2,
36–49; β1, 51–52; α3, 53–61; α4, 63–77; β2, 80–85;
β3, 88–96; α5, 97–119; α6, 124–139).
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Figure 2.
Fig. 2. BldR dimer structure with one monomer shown in red
and the other shown in green. Residues involved in polar
interactions at the dimer interface are also shown.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2009,
388,
559-569)
copyright 2009.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Peng,
X.Ao,
Y.X.Liang,
and
Q.She
(2011).
Archaeal promoter architecture and mechanism of gene activation.
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Biochem Soc Trans, 39,
99.
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H.Wade
(2010).
MD recognition by MDR gene regulators.
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Curr Opin Struct Biol, 20,
489-496.
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I.C.Perera,
and
A.Grove
(2010).
Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators.
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J Mol Cell Biol, 2,
243-254.
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S.Paytubi,
and
M.F.White
(2009).
The crenarchaeal DNA damage-inducible transcription factor B paralogue TFB3 is a general activator of transcription.
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Mol Microbiol, 72,
1487-1499.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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