Hbs

• Description: non-specific DNA-binding protein Hbsu
  
  

Gene name	hbs
Synonyms	dbpA, hupA
Essential	yes PubMed
Product	non-specific DNA-binding protein Hbsu
Function	DNA packaging, function of the signal recognition complex
Gene expression levels in SubtiExpress: hbs
MW, pI	9 kDa, 9.501
Gene length, protein length	276 bp, 92 aa
Immediate neighbours	folE, spoIVA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

DNA condensation/ segregation, essential genes, membrane proteins, phosphoproteins

This gene is a member of the following regulons

LexA regulon, SigH regulon

The gene

Basic information

• Locus tag: BSU22790

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU22790

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • Hbs-mediated untwisting of the DNA stimulates Nth endonuclease activity at AP sites PubMed

• Protein family: DbpA subfamily (according to Swiss-Prot)

• Paralogous protein(s): YonN

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-61 PubMed
  • phosphorylation on Thr-4 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • associated with the nucleoid in vegetative cells and forespores PubMed
  • membrane associated PubMed

Database entries

• BsubCyc: BSU22790

• Structure: 1HUU (Geobacillus stearothermophilus)

• UniProt: P08821

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hbs PubMed

• Expression browser: hbs PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • induced by DNA damage (LexA) PubMed
  • strongly repressed in response to glucose starvation in M9 medium PubMed

• Regulatory mechanism:
  • LexA: transcription repression PubMed

• Additional information:
  • mRNA is protected from degradation by RnjA by initiating ribosomes PubMed
  • Hbs is present with about 50,000 copies per genome in vegetative cells and spores, it is one of the most abundant proteins in B. subtilis PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 19917 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 41521 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab

• Antibody:

Labs working on this gene/protein

• Ciaran Condon, IBPC, Paris, France Homepage
• Mohamed Marahiel, University of Marburg, Germany Homepage

References

Original publications

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Christopher Collier, Cristina Machón, Geoff S Briggs, Wiep Klaas Smits, Panos Soultanas
Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites.
Nucleic Acids Res: 2012, 40(2);739-50
[PubMed:21954439] [WorldCat.org] [DOI] (I p)

Roula Daou-Chabo, Ciarán Condon
RNase J1 endonuclease activity as a probe of RNA secondary structure.
RNA: 2009, 15(7);1417-25
[PubMed:19458035] [WorldCat.org] [DOI] (I p)

Roula Daou-Chabo, Nathalie Mathy, Lionel Bénard, Ciarán Condon
Ribosomes initiating translation of the hbs mRNA protect it from 5'-to-3' exoribonucleolytic degradation by RNase J1.
Mol Microbiol: 2009, 71(6);1538-50
[PubMed:19210617] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

M A Ross, P Setlow
The Bacillus subtilis HBsu protein modifies the effects of alpha/beta-type, small acid-soluble spore proteins on DNA.
J Bacteriol: 2000, 182(7);1942-8
[PubMed:10715001] [WorldCat.org] [DOI] (P p)

S Fernández, J C Alonso
Bacillus subtilis sequence-independent DNA-binding and DNA-bending protein Hbsu negatively controls its own synthesis.
Gene: 1999, 231(1-2);187-93
[PubMed:10231583] [WorldCat.org] [DOI] (P p)

P Köhler, M A Marahiel
Mutational analysis of the nucleoid-associated protein HBsu of Bacillus subtilis.
Mol Gen Genet: 1998, 260(5);487-91
[PubMed:9894920] [WorldCat.org] [DOI] (P p)

S Fernández, F Rojo, J C Alonso
The Bacillus subtilis chromatin-associated protein Hbsu is involved in DNA repair and recombination.
Mol Microbiol: 1997, 23(6);1169-79
[PubMed:9106208] [WorldCat.org] [DOI] (P p)

P Köhler, M A Marahiel
Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis.
J Bacteriol: 1997, 179(6);2060-4
[PubMed:9068655] [WorldCat.org] [DOI] (P p)

B Micka, M A Marahiel
The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis.
Biochimie: 1992, 74(7-8);641-50
[PubMed:1382620] [WorldCat.org] [DOI] (P p)

B Micka, N Groch, U Heinemann, M A Marahiel
Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu.
J Bacteriol: 1991, 173(10);3191-8
[PubMed:1902464] [WorldCat.org] [DOI] (P p)