Transcriptional regulation of adhesive properties of Bacillus subtilis to extracellular matrix proteins through the fibronectin-binding protein YloA. 2017

Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
Departamento de Microbiología, Área Microbiología Básica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, CONICET - Rosario, Rosario, Argentina.

Bacterial adherence to extracellular matrix proteins (ECMp) plays important roles during host-pathogen interaction, however its genetic regulation remains poorly understood. yloA of the model bacterium Bacillus subtilis shows high homology to genes encoding fibronectin-binding proteins of Gram-positive pathogens. Here, we characterized the regulatory network of YloA-dependent adhesive properties of the probiotic B. subtilis natto (Bsn). YloA-proficient, but not YloA-deficient, Bsn specifically bound to ECMp in a concentration-dependent manner and were proficient in biofilm formation. yloA expression showed a continuous increase in activity during the growth phase and decreased during the stationary phase. The transcription factors AbrB and DegU downregulated yloA expression during the logarithmic and stationary growth phases respectively. Analysis of the yloA promoter region revealed the presence of AT-rich direct and inverted repeats previously reported to function as DegU-recognized binding sites. In spo0A cells, yloA expression was completely turned off because of upregulation of AbrB throughout growth. Accordingly, DNase I footprinting analysis confirmed that AbrB bound to the promoter region of yloA. Interestingly, Bsn bound fibronectin with higher affinity, lower Kd, than several bacterial pathogens and competitively excluded them from binding to immobilized-fibronectin, a finding that might be important for the anti-infective properties of B. subtilis and its relatives.

UI MeSH Term Description Entries
D010802 Phylogeny The relationships of groups of organisms as reflected by their genetic makeup. Community Phylogenetics,Molecular Phylogenetics,Phylogenetic Analyses,Phylogenetic Analysis,Phylogenetic Clustering,Phylogenetic Comparative Analysis,Phylogenetic Comparative Methods,Phylogenetic Distance,Phylogenetic Generalized Least Squares,Phylogenetic Groups,Phylogenetic Incongruence,Phylogenetic Inference,Phylogenetic Networks,Phylogenetic Reconstruction,Phylogenetic Relatedness,Phylogenetic Relationships,Phylogenetic Signal,Phylogenetic Structure,Phylogenetic Tree,Phylogenetic Trees,Phylogenomics,Analyse, Phylogenetic,Analysis, Phylogenetic,Analysis, Phylogenetic Comparative,Clustering, Phylogenetic,Community Phylogenetic,Comparative Analysis, Phylogenetic,Comparative Method, Phylogenetic,Distance, Phylogenetic,Group, Phylogenetic,Incongruence, Phylogenetic,Inference, Phylogenetic,Method, Phylogenetic Comparative,Molecular Phylogenetic,Network, Phylogenetic,Phylogenetic Analyse,Phylogenetic Clusterings,Phylogenetic Comparative Analyses,Phylogenetic Comparative Method,Phylogenetic Distances,Phylogenetic Group,Phylogenetic Incongruences,Phylogenetic Inferences,Phylogenetic Network,Phylogenetic Reconstructions,Phylogenetic Relatednesses,Phylogenetic Relationship,Phylogenetic Signals,Phylogenetic Structures,Phylogenetic, Community,Phylogenetic, Molecular,Phylogenies,Phylogenomic,Reconstruction, Phylogenetic,Relatedness, Phylogenetic,Relationship, Phylogenetic,Signal, Phylogenetic,Structure, Phylogenetic,Tree, Phylogenetic
D011401 Promoter Regions, Genetic DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes. rRNA Promoter,Early Promoters, Genetic,Late Promoters, Genetic,Middle Promoters, Genetic,Promoter Regions,Promoter, Genetic,Promotor Regions,Promotor, Genetic,Pseudopromoter, Genetic,Early Promoter, Genetic,Genetic Late Promoter,Genetic Middle Promoters,Genetic Promoter,Genetic Promoter Region,Genetic Promoter Regions,Genetic Promoters,Genetic Promotor,Genetic Promotors,Genetic Pseudopromoter,Genetic Pseudopromoters,Late Promoter, Genetic,Middle Promoter, Genetic,Promoter Region,Promoter Region, Genetic,Promoter, Genetic Early,Promoter, rRNA,Promoters, Genetic,Promoters, Genetic Middle,Promoters, rRNA,Promotor Region,Promotors, Genetic,Pseudopromoters, Genetic,Region, Genetic Promoter,Region, Promoter,Region, Promotor,Regions, Genetic Promoter,Regions, Promoter,Regions, Promotor,rRNA Promoters
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D005109 Extracellular Matrix A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere. Matrix, Extracellular,Extracellular Matrices,Matrices, Extracellular
D005353 Fibronectins Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins. Cold-Insoluble Globulins,LETS Proteins,Fibronectin,Opsonic Glycoprotein,Opsonic alpha(2)SB Glycoprotein,alpha 2-Surface Binding Glycoprotein,Cold Insoluble Globulins,Globulins, Cold-Insoluble,Glycoprotein, Opsonic,Proteins, LETS,alpha 2 Surface Binding Glycoprotein
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001412 Bacillus subtilis A species of gram-positive bacteria that is a common soil and water saprophyte. Natto Bacteria,Bacillus subtilis (natto),Bacillus subtilis subsp. natto,Bacillus subtilis var. natto
D001422 Bacterial Adhesion Physicochemical property of fimbriated (FIMBRIAE, BACTERIAL) and non-fimbriated bacteria of attaching to cells, tissue, and nonbiological surfaces. It is a factor in bacterial colonization and pathogenicity. Adhesion, Bacterial,Adhesions, Bacterial,Bacterial Adhesions
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial

Related Publications

Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
February 2014, Anaerobe,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
October 1982, Microbiologica,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
November 1996, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
February 1996, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
November 1986, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
February 2004, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
June 1994, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
June 1999, Molecular microbiology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
August 1994, Journal of bacteriology,
Facundo Rodriguez Ayala, and Carlos Bauman, and Marco Bartolini, and Ester Saball, and Marcela Salvarrey, and Cecilia Leñini, and Sebastián Cogliati, and Mark Strauch, and Roberto Grau
January 1989, Folia microbiologica,
Copied contents to your clipboard!