» Articles » PMID: 34417623

The Bacterial Iron Sensor IdeR Recognizes Its DNA Targets by Indirect Readout

Overview
Specialty Biochemistry
Date 2021 Aug 21
PMID 34417623
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

The iron-dependent regulator IdeR is the main transcriptional regulator controlling iron homeostasis genes in Actinobacteria, including species from the Corynebacterium, Mycobacterium and Streptomyces genera, as well as the erythromycin-producing bacterium Saccharopolyspora erythraea. Despite being a well-studied transcription factor since the identification of the Diphtheria toxin repressor DtxR three decades ago, the details of how IdeR proteins recognize their highly conserved 19-bp DNA target remain to be elucidated. IdeR makes few direct contacts with DNA bases in its target sequence, and we show here that these contacts are not required for target recognition. The results of our structural and mutational studies support a model wherein IdeR mainly uses an indirect readout mechanism, identifying its targets via the sequence-dependent DNA backbone structure rather than through specific contacts with the DNA bases. Furthermore, we show that IdeR efficiently recognizes a shorter palindromic sequence corresponding to a half binding site as compared to the full 19-bp target previously reported, expanding the number of potential target genes controlled by IdeR proteins.

Citing Articles

Structural basis for transcription activation through cooperative recruitment of MntR.

Shi H, Fu Y, Kodyte V, Andreas A, Sachla A, Miller K Nat Commun. 2025; 16(1):2204.

PMID: 40044701 PMC: 11882963. DOI: 10.1038/s41467-025-57412-6.


Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.

Capdevila D, Rondon J, Edmonds K, Rocchio J, Villarruel Dujovne M, Giedroc D Chem Rev. 2024; 124(24):13574-13659.

PMID: 39658019 PMC: 11672702. DOI: 10.1021/acs.chemrev.4c00264.


Identification, characterization and classification of prokaryotic nucleoid-associated proteins.

Schwab S, Dame R Mol Microbiol. 2024; 123(3):206-217.

PMID: 39039769 PMC: 11894785. DOI: 10.1111/mmi.15298.


The molecular mechanisms of the bacterial iron sensor IdeR.

Marcos-Torres F, Juniar L, Griese J Biochem Soc Trans. 2023; 51(3):1319-1329.

PMID: 37140254 PMC: 10317159. DOI: 10.1042/BST20221539.


Structural Dynamics of the MntR Transcription Factor Is Locked by Mn Binding.

Jelic Matosevic Z, Radman K, Loubser J, Crnolatac I, Piantanida I, Cukrowski I Int J Mol Sci. 2023; 24(2).

PMID: 36674477 PMC: 9861239. DOI: 10.3390/ijms24020957.


References
1.
Gumerov V, Ortega D, Adebali O, Ulrich L, Zhulin I . MiST 3.0: an updated microbial signal transduction database with an emphasis on chemosensory systems. Nucleic Acids Res. 2019; 48(D1):D459-D464. PMC: 6943060. DOI: 10.1093/nar/gkz988. View

2.
Chen C, White A, Love J, Murphy J, Ringe D . Methyl groups of thymine bases are important for nucleic acid recognition by DtxR. Biochemistry. 2000; 39(34):10397-407. DOI: 10.1021/bi0009284. View

3.
Schmitt M, Holmes R . Analysis of diphtheria toxin repressor-operator interactions and characterization of a mutant repressor with decreased binding activity for divalent metals. Mol Microbiol. 1993; 9(1):173-81. DOI: 10.1111/j.1365-2958.1993.tb01679.x. View

4.
Pan Q, Tong Y, Han Y, Ye B . Two amino acids missing of MtrA resulted in increased erythromycin level and altered phenotypes in Saccharopolyspora erythraea. Appl Microbiol Biotechnol. 2019; 103(11):4539-4548. DOI: 10.1007/s00253-019-09825-9. View

5.
Staron A, Sofia H, Dietrich S, Ulrich L, Liesegang H, Mascher T . The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) sigma factor protein family. Mol Microbiol. 2009; 74(3):557-81. DOI: 10.1111/j.1365-2958.2009.06870.x. View