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ArsR DNA-binding transcriptional repressor

Synonyms: ArsR-antimonite, ArsR-arsenite, ArsR
Summary:
ArsR negatively controls the expression of the genes involved in arsenical and antimonite metals resistance whose expression is induced in the presence of these metals [2, 3, 4, 5] This protein is autoregulated; arsR is the first gene in the arsRBC operon that it regulates [5] ArsR belongs to the ArsR/SmtB family of transcriptional regulators that respond to a variety of metals [1, 6] This family regulates the intracellular bioavailability of metal ions both inside and outside the host [6] ArsR has a helix-turn-helix motif for DNA binding, a metal-binding site [7] and a dimerization domain [8] The inducer-binding sites for the members of this family appear to have arisen by convergent evolution [9] In ArsR the inducer-binding site contains three cysteine residues that bind arsenite and antimonite specifically and with high affinity [7, 10] Dimerization of ArsR is required for its DNA binding and its ability to act as a transcriptional repressor [8] The dimer recognizes and binds to a 12-2-12 inverted repeat [1, 3] but the binding of arsenic or antimonite to ArsR causes a conformational change, leading to dissociation from DNA and hence derepression [10] The high-arsenic-mediated induction of ArsR binding requires that the ArsR binding sequence be placed at the first binding sequence; however, no such preference was observed for the second binding sequence [11] The nonconsensus base pairs of the ArsR transcription regulator could have a profound influence on protein binding and may also modulate post-binding function [11] The chromosomal ArsR shows 75% identity to ArsR of Escherichia coli plasmid R773 and 26% identity to staphylococcal plasmid pI258 and pSX267 ArsR proteins [4] ArsR when overexpressed has the capacity to remove arsenic species from contaminated water [12, 13] ArsR: homologous to "arsenate inducibility regulator" [5] Review: [1, 6] Read more >


Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence Confidence level (C: Confirmed, S: Strong, W: Weak) References
ArsR Functional   Apo nd nd nd
ArsR-antimonite Non-Functional Allosteric Holo nd nd nd
ArsR-arsenite Non-Functional Allosteric Holo nd nd nd
Evolutionary Family: ArsR
TFBs length: 24
Sensing class: External sensing using transported metabolites
Connectivity class: Local Regulator
Gene name: arsR
  Genome position: 3648528-3648881
  Length: 354 bp / 117 aa
Operon name: arsRBC
TU(s) encoding the TF:
Transcription unit        Promoter
arsRBC
arsRp


Regulon       
Regulated gene(s) arsB, arsC, arsR
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
detoxification (2)
The Arsenite-Antimonite (Ars) Efflux Family (1)
membrane (1)
Transcription related (1)
repressor (1)
Read more >
Regulated operon(s) arsRBC
First gene in the operon(s) arsR
Simple and complex regulons ArsR
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)
[ArsR,-](1)


Transcription factor regulation    


Transcription factor binding sites (TFBSs) arrangements
      

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence LeftPos RightPos Evidence Confidence level (C: Confirmed, S: Strong, W: Weak) References
  ArsR repressor arsRp Sigma70 -41.5 -57.5 arsR, arsB, arsC
acacattcgtTAAGTCATATATGTTTTTGACTTAtccgcttcga
 3648459 3648482 [EXP-IEP-GENE-EXPRESSION-ANALYSIS], [COMP-AINF-SIMILAR-TO-CONSENSUS], [EXP-IDA-BINDING-OF-PURIFIED-PROTEINS] S [1], [1], [2], [2], [3], [3]


Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
Promoter-target gene evolutionary conservation


Evidence    

 [EXP-IEP-GENE-EXPRESSION-ANALYSIS] Gene expression analysis

 [COMP-AINF-SIMILAR-TO-CONSENSUS] Automated inference based on similarity to consensus sequences

 [EXP-IDA-BINDING-OF-PURIFIED-PROTEINS] Binding of purified proteins


Reference(s)    

 [1] Busenlehner LS., Pennella MA., Giedroc DP., 2003, The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance., FEMS Microbiol Rev 27(2-3):131-43

 [2] Cai J., DuBow MS., 1996, Expression of the Escherichia coli chromosomal ars operon., Can J Microbiol 42(7):662-71

 [3] Xu C., Shi W., Rosen BP., 1996, The chromosomal arsR gene of Escherichia coli encodes a trans-acting metalloregulatory protein., J Biol Chem 271(5):2427-32

 [4] Carlin A, Shi W, Dey S, Rosen BP, 1995, The ars operon of Escherichia coli confers arsenical and antimonial resistance., J Bacteriol, 177(4):981 10.1128/jb.177.4.981-986.1995

 [5] Diorio C., Cai J., Marmor J., Shinder R., DuBow MS., 1995, An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria., J Bacteriol 177(8):2050-6

 [6] Saha RP, Samanta S, Patra S, Sarkar D, Saha A, Singh MK, 2017, Metal homeostasis in bacteria: the role of ArsR-SmtB family of transcriptional repressors in combating varying metal concentrations in the environment., Biometals, 30(4):459 10.1007/s10534-017-0020-3

 [7] Shi W., Wu J., Rosen BP., 1994, Identification of a putative metal binding site in a new family of metalloregulatory proteins., J Biol Chem 269(31):19826-9

 [8] Xu C, Rosen BP, 1997, Dimerization is essential for DNA binding and repression by the ArsR metalloregulatory protein of Escherichia coli., J Biol Chem, 272(25):15734 10.1074/jbc.272.25.15734

 [9] Qin J, Fu HL, Ye J, Bencze KZ, Stemmler TL, Rawlings DE, Rosen BP, 2007, Convergent evolution of a new arsenic binding site in the ArsR/SmtB family of metalloregulators., J Biol Chem, 282(47):34346 10.1074/jbc.M706565200

 [10] Shi W, Dong J, Scott RA, Ksenzenko MY, Rosen BP, 1996, The role of arsenic-thiol interactions in metalloregulation of the ars operon., J Biol Chem, 271(16):9291 10.1074/jbc.271.16.9291

 [11] Chen X, Jiang X, Tie C, Yoo J, Wang Y, Xu M, Sun G, Guo J, Li X, 2019, Contribution of nonconsensus base pairs within ArsR binding sequences toward ArsR-DNA binding and arsenic-mediated transcriptional induction., J Biol Eng, 13(None):53 10.1186/s13036-019-0181-4

 [12] Kostal J, Yang R, Wu CH, Mulchandani A, Chen W, 2004, Enhanced arsenic accumulation in engineered bacterial cells expressing ArsR., Appl Environ Microbiol, 70(8):4582 10.1128/AEM.70.8.4582-4587.2004

 [13] Yang T, Liu JW, Gu C, Chen ML, Wang JH, 2013, Expression of arsenic regulatory protein in Escherichia coli for selective accumulation of methylated arsenic species., ACS Appl Mater Interfaces, 5(7):2767 10.1021/am400578y


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