Regulation of the lic Operon ofBacillus subtilis and Characterization of Potential Phosphorylation Sites of the LicR Regulator Protein by Site-Directed Mutagenesis

Tobisch, Steffen; Stülke, Jörg; Hecker, Michael

doi:10.1128/jb.181.16.4995-5003.1999

Cited by 56 publications

(22 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Apart from the artefactual expression of the spoIIM gene (see Fig. 1, legend) the most dramatically induced genes in the fur mutant are the lic operon encoding enzymes for lichenan utilization (Tobisch et al ., 1999). The significance of this finding is not yet clear.…”

Section: Discussionmentioning

confidence: 99%

Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon

Baichoo

Wang

et al. 2002

Molecular Microbiology

237

268

View full text Add to dashboard Cite

SummaryThe Bacillus subtilis ferric uptake repressor (Fur) protein coordinates a global transcriptional response to iron starvation. We have used DNA microarrays to define the Fur regulon and the iron starvation stimulon. We identify 20 operons (containing 39 genes) that are derepressed both by mutation of fur and by treatment of cells with the iron chelator 2,2 ¢ ¢ ¢ ¢ -dipyridyl. These operons are direct targets of Fur regulation as judged by DNase I footprinting. Analyses of lacZ reporter fusions to six Fur-regulated promoter regions reveal that repression is highly selective for iron. In addition to the Fur regulon, iron starvation induces members of the PerR regulon and leads to reduced expression of cytochromes. However, we did not find any evidence for genes that are directly activated by Fur or repressed by Fur under iron-limiting conditions. Although genome searches using the 19 bp Fur box consensus are useful in identifying candidate Fur-regulated genes, some genes associated with Fur boxes are not demonstrably regulated by Fur, whereas other genes are regulated from sites with little apparent similarity to the conventional Fur consensus.

show abstract

Section: Discussionmentioning

confidence: 99%

Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon

Baichoo

Wang

et al. 2002

Molecular Microbiology

237

268

View full text Add to dashboard Cite

show abstract

“…The simplest versions contain an N-terminal wHTH domain fused to a C-terminal PRD domain. The more complex forms contain more than one PRD domains, or fusions to NtrC-like AAA+ domains and PTS system EIIB domains, which determine sugar specificity [95,96] (Fig. 3).…”

Section: Architectures Related To Two-component Pts and Serine/threomentioning

confidence: 99%

“…3). The B. subtilis LicR protein contains an N-terminal HTH fused to two PRDs and both EIIB and EIIA components of the PTS system [95,96], indicating that it is a multi-functional protein that directly regulates both sugar uptake and transcription of sugar-utilization genes. The 3H domain, which is related to the HPr domain of the PTS system, is also found fused to BirA-related wHTH domain in several bacterial proteins typified by Tm1602 from Thermotoga maritima [97].…”

Section: Architectures Related To Two-component Pts and Serine/threomentioning

confidence: 99%

The many faces of the helix-turn-helix domain: Transcription regulation and beyond

Aravind

Anantharaman

Balaji

et al. 2005

FEMS Microbiology Reviews

486

436

View full text Add to dashboard Cite

The helix-turn-helix (HTH) domain is a common denominator in basal and specific transcription factors from the three super-kingdoms of life. At its core, the domain comprises of an open tri-helical bundle, which typically binds DNA with the 3rd helix. Drawing on the wealth of data that has accumulated over two decades since the discovery of the domain, we present an overview of the natural history of the HTH domain from the viewpoint of structural analysis and comparative genomics. In structural terms, the HTH domains have developed several elaborations on the basic 3-helical core, such as the tetra-helical bundle, the winged-helix and the ribbon-helix-helix type configurations. In functional terms, the HTH domains are present in the most prevalent transcription factors of all prokaryotic genomes and some eukaryotic genomes. They have been recruited to a wide range of functions beyond transcription regulation, which include DNA repair and replication, RNA metabolism and protein-protein interactions in diverse signaling contexts. Beyond their basic role in mediating macromolecular interactions, the HTH domains have also been incorporated into the catalytic domains of diverse enzymes. We discuss the general domain architectural themes that have arisen amongst the HTH domains as a result of their recruitment to these diverse functions. We present a natural classification, higher-order relationships and phyletic pattern analysis of all the major families of HTH domains. This reconstruction suggests that there were at least 6-11 different HTH domains in the last universal common ancestor of all life forms, which covered much of the structural diversity and part of the functional versatility of the extant representatives of this domain. In prokaryotes the total number of HTH domains per genome shows a strong power-equation type scaling with the gene number per genome. However, the HTH domains in two-component signaling pathways show a linear scaling with gene number, in contrast to the non-linear scaling of HTH domains in single-component systems and sigma factors. These observations point to distinct evolutionary forces in the emergence of different signaling systems with HTH transcription factors. The archaea and bacteria share a number of ancient families of specific HTH transcription factors. However, they do not share any orthologous HTH proteins in the basal transcription apparatus. This differential relationship of their basal and specific transcriptional machinery poses an apparent conundrum regarding the origins of their transcription apparatus.

show abstract

“…The simplest versions contain an N‐terminal wHTH domain fused to a C‐terminal PRD domain. The more complex forms contain more than one PRD domains, or fusions to NtrC‐like AAA+ domains and PTS system EIIB domains, which determine sugar specificity [95,96] (Fig. 3).…”

Section: General and Specific Aspects Of The Domain Architectures Ofmentioning

confidence: 99%

“…3). The B. subtilis LicR protein contains an N‐terminal HTH fused to two PRDs and both EIIB and EIIA components of the PTS system [95,96], indicating that it is a multi‐functional protein that directly regulates both sugar uptake and transcription of sugar‐utilization genes. The 3H domain, which is related to the HPr domain of the PTS system, is also found fused to BirA‐related wHTH domain in several bacterial proteins typified by Tm1602 from Thermotoga maritima [97].…”

Section: General and Specific Aspects Of The Domain Architectures Ofmentioning

confidence: 99%

The many faces of the helix-turn-helix domain: Transcription regulation and beyond

Aravind¹,

Anantharaman²,

Balaji³

et al. 2005

FEMS Microbiol Rev

360

196

View full text Add to dashboard Cite

The helix-turn-helix (HTH) domain is a common denominator in basal and specific transcription factors from the three superkingdoms of life. At its core, the domain comprises of an open tri-helical bundle, which typically binds DNA with the 3rd helix. Drawing on the wealth of data that has accumulated over two decades since the discovery of the domain, we present an overview of the natural history of the HTH domain from the viewpoint of structural analysis and comparative genomics. In structural terms, the HTH domains have developed several elaborations on the basic 3-helical core, such as the tetra-helical bundle, the winged-helix and the ribbon-helix-helix type configurations. In functional terms, the HTH domains are present in the most prevalent transcription factors of all prokaryotic genomes and some eukaryotic genomes. They have been recruited to a wide range of functions beyond transcription regulation, which include DNA repair and replication, RNA metabolism and protein-protein interactions in diverse signaling contexts. Beyond their basic role in mediating macromolecular interactions, the HTH domains have also been incorporated into the catalytic domains of diverse enzymes. We discuss the general domain architectural themes that have arisen amongst the HTH domains as a result of their recruitment to these diverse functions. We present a natural classification, higher-order relationships and phyletic pattern analysis of all the major families of HTH domains. This reconstruction suggests that there were at least 6-11 different HTH domains in the last universal common ancestor of all life forms, which covered much of the structural diversity and part of the functional versatility of the extant representatives of this domain. In prokaryotes the total number of HTH domains per genome shows a strong power-equation type scaling with the gene number per genome. However, the HTH domains in two-component signaling pathways show a linear scaling with gene number, in contrast to the non-linear scaling of HTH domains in single-component systems and sigma factors. These observations point to distinct evolutionary forces in the emergence of different signaling systems with HTH transcription factors. The archaea and bacteria share a number of ancient families of specific HTH transcription factors. However, they do not share any orthologous HTH proteins in the basal transcription apparatus. This differential relationship of their basal and specific transcriptional machinery poses an apparent conundrum regarding the origins of their transcription apparatus.

show abstract

Regulation of the lic Operon ofBacillus subtilis and Characterization of Potential Phosphorylation Sites of the LicR Regulator Protein by Site-Directed Mutagenesis

Cited by 56 publications

References 45 publications

Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon

Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon

The many faces of the helix-turn-helix domain: Transcription regulation and beyond

The many faces of the helix-turn-helix domain: Transcription regulation and beyond

Contact Info

Product

Resources

About