» Articles » PMID: 15051891

HetR Homodimer is a DNA-binding Protein Required for Heterocyst Differentiation, and the DNA-binding Activity is Inhibited by PatS

Overview
Specialty Science
Date 2004 Mar 31
PMID 15051891
Citations 75
Authors
Affiliations
Soon will be listed here.
Abstract

HetR plays a key role in regulation of heterocyst differentiation. When the Cys-48 residue of the HetR from Anabaena sp. PCC 7120 was replaced with an Ala residue, the mutant HetR (HetR(C48A)) could not dimerize, indicating that HetR forms a homodimer through a disulfide bond. The Anabaena strain C48, containing the hetRc48a gene, could not produce HetR homodimer and failed to form heterocyst. We show that HetR is a DNA-binding protein and that its homodimerization is required for the DNA binding. HetR binds the promoter regions of hetR, hepA, and patS, suggesting a direct control of the expression of these genes by HetR. We present evidence that shows that the up-regulation of patS and hetR depends on DNA binding by HetR dimer. The pentapeptide RGSGR, which is present at the C terminus of PatS and blocks heterocyst formation, inhibits the DNA binding of HetR and prevents hetR up-regulation.

Citing Articles

R-DeeP/TripepSVM identifies the RNA-binding OB-fold-like protein PatR as regulator of heterocyst patterning.

Brenes-Alvarez M, Ropp H, Papagiannidis D, Potel C, Stein F, Scholz I Nucleic Acids Res. 2024; 53(3).

PMID: 39698830 PMC: 11797042. DOI: 10.1093/nar/gkae1247.


PatU3 plays a central role in coordinating cell division and differentiation in pattern formation of filamentous cyanobacterium Nostoc sp. PCC 7120.

Yin L, Zheng Z, Li Y, Li X, Cheng D, Dong C Sci China Life Sci. 2023; 66(12):2896-2909.

PMID: 37505430 DOI: 10.1007/s11427-023-2380-1.


Evaluating EcxR for Its Possible Role in Gene Regulation.

Liu H, Knox C, Jakkula L, Wang Y, Peddireddi L, Ganta R Int J Mol Sci. 2022; 23(21).

PMID: 36361509 PMC: 9657007. DOI: 10.3390/ijms232112719.


Mathematical models of nitrogen-fixing cell patterns in filamentous cyanobacteria.

Casanova-Ferrer P, Munoz-Garcia J, Ares S Front Cell Dev Biol. 2022; 10:959468.

PMID: 36187490 PMC: 9523125. DOI: 10.3389/fcell.2022.959468.


Terminal heterocyst differentiation in the Anabaena patA mutant as a result of post-transcriptional modifications and molecular leakage.

Casanova-Ferrer P, Ares S, Munoz-Garcia J PLoS Comput Biol. 2022; 18(8):e1010359.

PMID: 35969646 PMC: 9410556. DOI: 10.1371/journal.pcbi.1010359.


References
1.
Black T, Wolk C . Analysis of a Het- mutation in Anabaena sp. strain PCC 7120 implicates a secondary metabolite in the regulation of heterocyst spacing. J Bacteriol. 1994; 176(8):2282-92. PMC: 205350. DOI: 10.1128/jb.176.8.2282-2292.1994. View

2.
Golden J, Yoon H . Heterocyst development in Anabaena. Curr Opin Microbiol. 2003; 6(6):557-63. DOI: 10.1016/j.mib.2003.10.004. View

3.
Fu G, Smith M, Markovitz D . Bacterial protease Lon is a site-specific DNA-binding protein. J Biol Chem. 1997; 272(1):534-8. View

4.
Adams D . Heterocyst formation in cyanobacteria. Curr Opin Microbiol. 2000; 3(6):618-24. DOI: 10.1016/s1369-5274(00)00150-8. View

5.
Gottesman S . Regulation by proteolysis: developmental switches. Curr Opin Microbiol. 1999; 2(2):142-7. DOI: 10.1016/S1369-5274(99)80025-3. View