Difference between revisions of "RnhC"
| Line 52: | Line 52: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| − | |||
=The protein= | =The protein= | ||
| Line 78: | Line 75: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
| + | ** RnhC interacts with the [[RNA polymerase]] {{PubMed|21710567}} | ||
* '''Localization:''' cytoplasm (according to Swiss-Prot) | * '''Localization:''' cytoplasm (according to Swiss-Prot) | ||
| Line 128: | Line 126: | ||
<pubmed>19228197 </pubmed> | <pubmed>19228197 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| + | '''Additional publications:''' {{PubMed|21710567}} | ||
<pubmed>8969504 10094689 9888800 17905985 </pubmed> | <pubmed>8969504 10094689 9888800 17905985 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:51, 29 June 2011
- Description: RNase HIII, endoribonuclease
| Gene name | rnhC |
| Synonyms | ysgB |
| Essential | no |
| Product | Mg2+-dependent RNase HIII |
| Function | endonucleolytic cleavage of RNA in RNA-DNA hybrid molecules |
| MW, pI | 33 kDa, 10.07 |
| Gene length, protein length | 939 bp, 313 aa |
| Immediate neighbours | zapA, pheT |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28620
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Endonucleolytic cleavage to 5'-phosphomonoester (according to Swiss-Prot)
- Protein family: RnhC subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- RnhC interacts with the RNA polymerase PubMed
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 2D0B (complex with Mg2+, Geobacillus stearothermophilus , 47% identity), 2D0A (Geobacillus stearothermophilus, 47% identity)
- UniProt: P94541
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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
Additional publications: PubMed
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)
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)
A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504]
[WorldCat.org]
[DOI]
(P p)
