Difference between revisions of "EpsD"
| Line 112: | Line 112: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}} | ** induction by sequestration of [[SinR]] by [[SinI]] or [[SlrA]] {{PubMed|15661000,19788541}} | ||
| + | ** 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}} | ||
** 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}} | ||
| Line 139: | Line 140: | ||
<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 20:29, 19 November 2011
- Description: extracellular polysaccharide synthesis
| Gene name | epsD |
| Synonyms | yveN |
| Essential | no |
| Product | unknown |
| Function | biofilm formation |
| Regulation of this protein in SubtiPathways: Biofilm | |
| MW, pI | 43 kDa, 8.732 |
| Gene length, protein length | 1143 bp, 381 aa |
| Immediate neighbours | epsE, epsC |
| 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
AbrB regulon, EAR riboswitch, SinR regulon
The gene
Basic information
- Locus tag: BSU34340
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: glycosyltransferase 1 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P71053
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
- induction by sequestration of SinR by SinI or SlrA 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
- 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
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
Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481]
[WorldCat.org]
[DOI]
(I p)
Original publications
The EAR RNA switch
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
