EurekaMag.com logo
+ Site Statistics
References:
54,215,046
Abstracts:
30,230,908
PMIDs:
28,215,208
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on LinkedInFollow on LinkedIn

+ Translate

Molecular domain organization of BldD, an essential transcriptional regulator for developmental process of Streptomyces coelicolor A3(2)



Molecular domain organization of BldD, an essential transcriptional regulator for developmental process of Streptomyces coelicolor A3(2)



Proteins 68(1): 344-352



A homodimeric protein, BldD is a key regulator for developmental process of Streptomyces coelicolor and the bldD mutant exhibits severely pleiotropic defects in the antibiotic production and morphological differentiation of the bacterium. In the present work, we approached domain organization of BldD, to structurally and functionally characterize the protein as a DNA-binding protein. We first observed a proteolytic cleavage of BldD by the cytoplasmic extracts of S. coelicolor, which was highly dependent on the developmental stage of the bacterium. The resulting fragment of BldD was identified by mass spectrometry as the N-terminal domain resistant to the proteolysis. Recombinant proteins corresponding to the intact BldD, the N-terminal domain (residues 1-79) and the rest part (C-terminal domain; residues 80-167) were used for comparative analyses by several spectroscopic, thermodynamic, and biochemical experiments, respectively. The results of circular dichroism and nuclear magnetic resonance spectroscopies certified each of the two determined domains could be regarded as an individual folding unit possessing an independent thermodynamic cooperativity. Structural interaction between the two domains was little observed in the DNA-free and DNA-bound states. Strikingly, it was revealed by gel permeation chromatography, chemical crosslink, gel mobility shift, and NMR-monitored DNA-binding experiments, that only the N-terminal domain is responsible for the dimerization as well as DNA-binding of BldD. Detailed inspection of the present results suggests that BldD function in a unique and complicated mode to totally regulate the diverse developmental stages of S. coelicolor.

(PDF emailed within 0-6 h: $19.90)

Accession: 013763073

Download citation: RISBibTeXText

PMID: 17427251

DOI: 10.1002/prot.21338



Related references

The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains. Proteins 82(6): 1093-1098, 2015

BldD is a direct regulator of key developmental genes in Streptomyces coelicolor A3(2). Molecular Microbiology 40(1): 257-269, 2001

BldD from Streptomyces coelicolor is a non-essential global regulator that binds its own promoter as a dimer. FEMS Microbiology Letters 225(1): 35-40, 8 August, 2003

Crystal structure of the DNA-binding domain of BldD, a central regulator of aerial mycelium formation in Streptomyces coelicolor A3(2). Molecular Microbiology 60(5): 1179-1193, 2006

Crystallization and preliminary X-ray crystallographic analysis of the DNA-binding domain of BldD from Streptomyces coelicolor A3(2). Acta Crystallographica. Section D, Biological Crystallography 60(Pt 6): 1115-1117, 2004

Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth. Molecular Microbiology 78(2): 361-379, 2011

Intramolecular interaction of the transcription factor BldD in Streptomyces coelicolor. Biophysical Journal 86(1): 82a, January, 2004

Expression of the melC operon in several Streptomyces strains is positively regulated by AdpA, an AraC family transcriptional regulator involved in morphological development in Streptomyces coelicolor. Journal of Bacteriology 187(9): 3180-3187, 2005

A transcriptional regulator of a pristinamycin resistance gene in Streptomyces coelicolor. Journal of Biological Chemistry 276(2): 1479-1485, 2000

A transcriptional regulator of a pristinamycin resistance gene in Streptomyces coelicolor. Journal of Biological Chemistry 276(2): 1479-1485, 2001

A new TetR family transcriptional regulator required for morphogenesis in Streptomyces coelicolor. Journal of Bacteriology 190(1): 61-67, 2007

DevA, a GntR-like transcriptional regulator required for development in Streptomyces coelicolor. Journal of Bacteriology 188(14): 5014-5023, 2006

Transcriptional activation of the pathway-specific regulator of the actinorhodin biosynthetic genes in Streptomyces coelicolor. Molecular Microbiology 58(1): 131-150, 2005