Difference between revisions of "Sandbox"
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− | * '''Description:''' | + | * '''Description:''' RNase J1<br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
|- | |- | ||
|style="background:#ABCDEF;" align="center"|'''Gene name''' | |style="background:#ABCDEF;" align="center"|'''Gene name''' | ||
− | |'' | + | |''rnjA '' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' '' | + | |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''ykqC'' |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Essential''' || | + | |style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || RNase J1 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || RNA processing |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || | + | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 61 kDa, 5.902 |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || | + | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1665 bp, 555 aa |
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[adeC]]'', ''[[ykzG]]'' |
|- | |- | ||
− | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS: | + | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB13326]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
|- | |- | ||
− | |colspan="2" | '''Genetic context''' <br/> [[Image: | + | |colspan="2" | '''Genetic context''' <br/> [[Image:ykqC_context.gif]] |
<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
|- | |- | ||
Line 38: | Line 38: | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
+ | |||
+ | essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] | ||
=== Database entries === | === Database entries === | ||
Line 43: | Line 45: | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
− | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+ | + | * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG11813] |
=== Additional information=== | === Additional information=== | ||
Line 52: | Line 54: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
− | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' endonuclease and 5'-3' exonuclease |
* '''Protein family:''' | * '''Protein family:''' | ||
− | * '''Paralogous protein(s):''' | + | * '''Paralogous protein(s):''' [[RnjB]] |
+ | |||
+ | === RNAs affected by ''rnjA'' === | ||
+ | |||
+ | ''[[hbs]]'', ''[[thrS]]'' | ||
=== Extended information on the protein === | === Extended information on the protein === | ||
Line 70: | Line 76: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''Interactions:''' [[RnjA]]-[[RnjB]], [[RnjA]]-[[PfkA]], [[RnjA]]-[[PnpA]], [[RnjA]]-[[Rny]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed] |
* '''Localization:''' Cytoplasm | * '''Localization:''' Cytoplasm | ||
Line 76: | Line 82: | ||
=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do;jsessionid=8B071C0C81B11ADEBA3DDC3FF3395811?structureId=3BK1 3BK1] (RNase J from ''Thermus thermophilus'') [http://www.pdb.org/pdb/explore/explore.do?structureId=3BK2 3BK2] (RNase J from ''Thermus thermophilus'', complex with UMP) |
* '''Swiss prot entry:''' | * '''Swiss prot entry:''' | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU14530] |
* '''E.C. number:''' | * '''E.C. number:''' | ||
=== Additional information=== | === Additional information=== | ||
+ | |||
+ | :* subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
+ | |||
+ | required for ''[[thrS]]'' RNA processing, involved in maturation of the 5’-end of the16S rRNA, subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
=Expression and regulation= | =Expression and regulation= | ||
Line 90: | Line 100: | ||
* '''Operon:''' | * '''Operon:''' | ||
− | * ''' | + | * '''Sigma factor:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 96: | Line 106: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | * '''Additional information:''' | + | * '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed], subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] |
=Biological materials = | =Biological materials = | ||
Line 108: | Line 118: | ||
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
− | * '''two-hybrid system:''' | + | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab |
* '''Antibody:''' | * '''Antibody:''' | ||
=Labs working on this gene/protein= | =Labs working on this gene/protein= | ||
+ | |||
+ | [[Harald Putzer]], IBPC Paris, France [http://www.ibpc.fr/UPR9073/putzer/recherches_harald.htm Homepage] | ||
+ | |||
+ | [[David Bechhofer]], Mount Sinai School, New York, USA [http://www.mountsinai.org/Research/Centers%20Laboratories%20and%20Programs/Bechhofer%20Laboratory?citype=Physician&ciid=Bechhofer%20David%20H%201255565 Homepage] | ||
+ | |||
+ | [[Ciaran Condon]], IBPC, Paris, France [http://www.ibpc.fr/UPR9073/condon/index_en.html Homepage] | ||
=Your additional remarks= | =Your additional remarks= | ||
Line 118: | Line 134: | ||
=References= | =References= | ||
+ | # Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed] | ||
+ | # Even, S., Pellegrini, O., Zig, L., Labas, V., Vinh, J., Brechemmier-Baey, D., and Putzer, H. (2005) Ribonucleases J1 and J2: Two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E. Nucl Acids Res 33, 2141-2152. [http://www.ncbi.nlm.nih.gov/sites/entrez/15831787 PubMed] | ||
+ | # de la Sierra-Gallay IL, Zig L, Jamalli A, Putzer H. (2008 Structural insights into the dual activity of RNase J. Nat. Struct. Mol. Biol. 15:206-212. [http://www.ncbi.nlm.nih.gov/sites/entrez/18204464 PubMed] | ||
+ | # Mäder, U., Zig, L., Kretschmer, J., Homuth, G., and Putzer, H. (2008) mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene expression on a global scale. Mol Microbiol 70, 183-196. [http://www.ncbi.nlm.nih.gov/sites/entrez/18713320 PubMed] | ||
+ | # Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press [http://www.ncbi.nlm.nih.gov/sites/entrez/19193632 PubMed] | ||
+ | # Hunt, A., Rawlins, J. P., Thomaides, H. B., and Errington, J. (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152, 2895-2907. [http://www.ncbi.nlm.nih.gov/sites/entrez/17005971 PubMed] | ||
+ | # Deikus, G., Condon, C. & Bechhofer, D. H. (2008). Role of ''Bacillus subtilis'' RNase J1 endonuclease and 5'-exonuclease activities in ''trp'' leader RNA turnover. J Biol Chem. 283:17158-17167. [http://www.ncbi.nlm.nih.gov/sites/entrez/18445592 PubMed] | ||
+ | # Mathy, N., Bénard, L., Pellegrini, O., Daou, R., Wen, T. & Condon, C. (2007). 5'-to-3' exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5' stability of mRNA. Cell 129:681-692. [http://www.ncbi.nlm.nih.gov/sites/entrez/17512403 PubMed] | ||
+ | # Britton et al. (2007) Maturation of the 5' end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1. Mol. Microbiol. 63: 127-138. [http://www.ncbi.nlm.nih.gov/sites/entrez/17229210 PubMed] | ||
+ | # Yao, S., Blaustein, J. B. & Bechhofer, D. H. (2007). Processing of ''Bacillus subtilis'' small cytoplasmic RNA: evidence for an additional endonuclease cleavage site. Nucleic Acids Res. 35:4464-4473. [http://www.ncbi.nlm.nih.gov/sites/entrez/17576666 PubMed] | ||
+ | # Daou-Chabo R, Mathy N, Bénard L, Condon C. (2009) Ribosomes initiating translation of the ''hbs'' mRNA protect it from 5'-to-3' exoribonucleolytic degradation by RNase J1. ''Mol. Microbiol.'' '''71:''' 1538-1550. [http://www.ncbi.nlm.nih.gov/sites/entrez/19210617 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 02:09, 30 April 2009
- Description: RNase J1
Gene name | rnjA |
Synonyms | ykqC |
Essential | yes PubMed |
Product | RNase J1 |
Function | RNA processing |
MW, pI | 61 kDa, 5.902 |
Gene length, protein length | 1665 bp, 555 aa |
Immediate neighbours | adeC, ykzG |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context ![]() This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: endonuclease and 5'-3' exonuclease
- Protein family:
- Paralogous protein(s): RnjB
RNAs affected by rnjA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: Cytoplasm
Database entries
- Structure: 3BK1 (RNase J from Thermus thermophilus) 3BK2 (RNase J from Thermus thermophilus, complex with UMP)
- Swiss prot entry:
- KEGG entry: [2]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
required for thrS RNA processing, involved in maturation of the 5’-end of the16S rRNA, subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed, subject to Clp-dependent proteolysis upon glucose starvation 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 Stülke lab
- Antibody:
Labs working on this gene/protein
Harald Putzer, IBPC Paris, France Homepage
David Bechhofer, Mount Sinai School, New York, USA Homepage
Ciaran Condon, IBPC, Paris, France Homepage
Your additional remarks
References
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- Even, S., Pellegrini, O., Zig, L., Labas, V., Vinh, J., Brechemmier-Baey, D., and Putzer, H. (2005) Ribonucleases J1 and J2: Two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E. Nucl Acids Res 33, 2141-2152. PubMed
- de la Sierra-Gallay IL, Zig L, Jamalli A, Putzer H. (2008 Structural insights into the dual activity of RNase J. Nat. Struct. Mol. Biol. 15:206-212. PubMed
- Mäder, U., Zig, L., Kretschmer, J., Homuth, G., and Putzer, H. (2008) mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene expression on a global scale. Mol Microbiol 70, 183-196. PubMed
- Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press PubMed
- Hunt, A., Rawlins, J. P., Thomaides, H. B., and Errington, J. (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152, 2895-2907. PubMed
- Deikus, G., Condon, C. & Bechhofer, D. H. (2008). Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease activities in trp leader RNA turnover. J Biol Chem. 283:17158-17167. PubMed
- Mathy, N., Bénard, L., Pellegrini, O., Daou, R., Wen, T. & Condon, C. (2007). 5'-to-3' exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5' stability of mRNA. Cell 129:681-692. PubMed
- Britton et al. (2007) Maturation of the 5' end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1. Mol. Microbiol. 63: 127-138. PubMed
- Yao, S., Blaustein, J. B. & Bechhofer, D. H. (2007). Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an additional endonuclease cleavage site. Nucleic Acids Res. 35:4464-4473. PubMed
- Daou-Chabo R, Mathy N, Bénard L, Condon C. (2009) Ribosomes initiating translation of the hbs mRNA protect it from 5'-to-3' exoribonucleolytic degradation by RNase J1. Mol. Microbiol. 71: 1538-1550. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed