Hbs

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  • 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
Hbs context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Hbs expression.png

Contents















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

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:

Database entries

  • Structure: 1HUU (Geobacillus stearothermophilus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Wolfgang Klein, Mohamed A Marahiel
Structure-function relationship and regulation of two Bacillus subtilis DNA-binding proteins, HBsu and AbrB.
J. Mol. Microbiol. Biotechnol.: 2002, 4(3);323-9
[PubMed:11931565] [WorldCat.org] (P p)

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] (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] (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] (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] (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] (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] (P p)

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