RnhB

• Description: RNase HII, endoribonuclease, responsible for removal of single rNMPs incorporated into DNA by DNA polymerase during DNA replication
  
  

Gene name	rnhB
Synonyms	rnh
Essential	no
Product	Mn2+-dependent RNase HII
Function	endonucleolytic cleavage of RNA in RNA-DNA hybrid molecules
Gene expression levels in SubtiExpress: rnhB
MW, pI	28 kDa, 5.518
Gene length, protein length	765 bp, 255 aa
Immediate neighbours	rbgA, ylqG
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 replication, Rnases

The gene

Basic information

• Locus tag: BSU16060

Phenotypes of a mutant

• increased mutation rate PubMed
• a rnhB rnhC double mutant grows poorly PubMed
• a rnhB mutS-mutL mutant is not viable PubMed

Database entries

• BsubCyc: BSU16060

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • Endonucleolytic cleavage to 5'-phosphomonoester (according to Swiss-Prot)
  • removal of single rNMPs incorporated into DNA by DNA polymerase during DNA replication PubMed

• Protein family: RNase HII family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU16060

• Structure:

• UniProt: O31744

• KEGG entry: [2]

• E.C. number: 3.1.26.4.

Expression and regulation

• Operon:

• Expression browser: rnhB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: BP423 (ΔrnhB::aphA3) available in Fabian Commichau's lab

• Expression vector: for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, expression from plasmid: pBP500 (E. coli amp & B. subtilis E/L) , available in Fabian Commichau's lab

• lacZ fusion:

• GFP fusion:

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

• Antibody:

References

Reviews

Karolina A Majorek, Stanislaw Dunin-Horkawicz, Kamil Steczkiewicz, Anna Muszewska, Marcin Nowotny, Krzysztof Ginalski, Janusz M Bujnicki
The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification.
Nucleic Acids Res: 2014, 42(7);4160-79
[PubMed:24464998] [WorldCat.org] [DOI] (I p)

Takashi Tadokoro, Shigenori Kanaya
Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.
FEBS J: 2009, 276(6);1482-93
[PubMed:19228197] [WorldCat.org] [DOI] (I p)

Original publications

Nina Y Yao, Jeremy W Schroeder, Olga Yurieva, Lyle A Simmons, Mike E O'Donnell
Cost of rNTP/dNTP pool imbalance at the replication fork.
Proc Natl Acad Sci U S A: 2013, 110(32);12942-7
[PubMed:23882084] [WorldCat.org] [DOI] (I p)

Sanae Fukushima, Mitsuhiro Itaya, Hiroaki Kato, Naotake Ogasawara, Hirofumi Yoshikawa
Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth.
J Bacteriol: 2007, 189(23);8575-83
[PubMed:17905985] [WorldCat.org] [DOI] (I p)

Mitsuru Haruki, Yasuo Tsunaka, Masaaki Morikawa, Shigenori Kanaya
Cleavage of a DNA-RNA-DNA/DNA chimeric substrate containing a single ribonucleotide at the DNA-RNA junction with prokaryotic RNases HII.
FEBS Lett: 2002, 531(2);204-8
[PubMed:12417313] [WorldCat.org] [DOI] (P p)

M Itaya, A Omori, S Kanaya, R J Crouch, T Tanaka, K Kondo
Isolation of RNase H genes that are essential for growth of Bacillus subtilis 168.
J Bacteriol: 1999, 181(7);2118-23
[PubMed:10094689] [WorldCat.org] [DOI] (P p)

N Ohtani, M Haruki, M Morikawa, R J Crouch, M Itaya, S Kanaya
Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: classification of RNases H into three families.
Biochemistry: 1999, 38(2);605-18
[PubMed:9888800] [WorldCat.org] [DOI] (P p)