Difference between revisions of "EpsK"
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=== Additional information=== | === Additional information=== | ||
| − | + | The gene was re-assembled due to sequencing error in original sequence (it encompasses the genes annotated as ''yvfA'' and ''yvfB'' in SubtiList) [http://www.ncbi.nlm.nih.gov/sites/entrez/15661000 PubMed] | |
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=The protein= | =The protein= | ||
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** the ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' operon is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}} | ** the ''[[epsA]]-[[epsB]]-[[epsC]]-[[epsD]]-[[epsE]]-[[epsF]]-[[epsG]]-[[epsH]]-[[epsI]]-[[epsJ]]-[[epsK]]-[[epsL]]-[[epsM]]-[[epsN]]-[[epsO]]'' operon is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}} | ||
** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
| + | ** the [[EAR riboswitch]] (eps-associated [[RNA switch]]) located between'' [[epsB]]'' and ''[[epsC]]'' mediates processive antitermination and allows expression of the long eps operon {{PubMed|20374491}} | ||
=Biological materials = | =Biological materials = | ||
| Line 141: | Line 139: | ||
<pubmed>20735481 </pubmed> | <pubmed>20735481 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| + | ===The EAR [[RNA switch]]=== | ||
| + | <pubmed>20374491 20230605 </pubmed> | ||
| + | ===Other original publications=== | ||
'''Additional publications:''' {{PubMed|20817675}} | '''Additional publications:''' {{PubMed|20817675}} | ||
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
Revision as of 20:31, 19 November 2011
- Description: extracellular polysaccharide synthesis
| Gene name | epsK |
| Synonyms | yvfA, yvfB |
| Essential | no |
| Product | unknown |
| Function | biofilm formation |
| Regulation of this protein in SubtiPathways: Biofilm | |
| MW, pI | |
| Gene length, protein length | 1515 bp, 505 aa |
| Immediate neighbours | epsL, epsJ |
| 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
biofilm formation, membrane proteins
This gene is a member of the following regulons
AbrB regulon, EAR riboswitch, SinR regulon
The gene
Basic information
- Locus tag: BSU34265
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The gene was re-assembled due to sequencing error in original sequence (it encompasses the genes annotated as yvfA and yvfB in SubtiList) PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P71060
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
- induction by sequestration of SinR by SinI or SlrA PubMed
- the epsA-epsB-epsC-epsD-epsE-epsF-epsG-epsH-epsI-epsJ-epsK-epsL-epsM-epsN-epsO operon is not expressed in a ymdB mutant PubMed
- the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed
- the EAR riboswitch (eps-associated RNA switch) located between epsB and epsC mediates processive antitermination and allows expression of the long eps operon PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Richard Losick, Harvard Univ., Cambridge, USA homepage
Your additional remarks
References
Reviews
Original publications
The EAR RNA switch
Irnov Irnov, Wade C Winkler
A regulatory RNA required for antitermination of biofilm and capsular polysaccharide operons in Bacillales.
Mol Microbiol: 2010, 76(3);559-75
[PubMed:20374491]
[WorldCat.org]
[DOI]
(I p)
Zasha Weinberg, Joy X Wang, Jarrod Bogue, Jingying Yang, Keith Corbino, Ryan H Moy, Ronald R Breaker
Comparative genomics reveals 104 candidate structured RNAs from bacteria, archaea, and their metagenomes.
Genome Biol: 2010, 11(3);R31
[PubMed:20230605]
[WorldCat.org]
[DOI]
(I p)
Other original publications
Additional publications: PubMed
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects Flagellin Expression and Biofilm Formation. J Bacteriol.: 2011, 193(21):5997-6007. PubMed:21856853
K Nagorska, A Ostrowski, K Hinc, I B Holland, M Obuchowski
Importance of eps genes from Bacillus subtilis in biofilm formation and swarming.
J Appl Genet: 2010, 51(3);369-81
[PubMed:20720312]
[WorldCat.org]
[DOI]
(I p)
Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168]
[WorldCat.org]
[DOI]
(I p)
Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568]
[WorldCat.org]
[DOI]
(P p)
Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695]
[WorldCat.org]
[DOI]
(P p)
Daniel B Kearns, Frances Chu, Steven S Branda, Roberto Kolter, Richard Losick
A master regulator for biofilm formation by Bacillus subtilis.
Mol Microbiol: 2005, 55(3);739-49
[PubMed:15661000]
[WorldCat.org]
[DOI]
(P p)
