Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1999-4-22
|
pubmed:databankReference | |
pubmed:abstractText |
We identified, in the facultative intracellular pathogen Listeria monocytogenes, a previously unknown Clp ATPase, unique among the HSP100 proteins because of the presence of a short N-terminal region with a potential zinc finger motif. This protein of 726 amino acids is highly homologous to ClpE of Bacillus subtilis, and is a member of a new subfamily of HSP100/Clp ATPases. The clpE gene is transcribed as a monocistronic mRNA from a typical consensus sigma A promoter. clpE is not stimulated by various stresses, but is upregulated in a clpC mutant. This is the first example of cross-regulation between Clp ATPases. By constructing a clpE mutant of L. monocytogenes, we found that ClpE is required for prolonged survival at 42 degrees C and is involved in the virulence of this pathogen. A double mutant deficient in both ClpE and ClpC was avirulent in a mouse model and completely eliminated in the liver. Electron microscopy studies did not show any morphological alterations in clpE or clpC mutants. In the clpE-clpC double mutant, however, cell division was affected, indicating that ClpE acts synergistically with ClpC in cell septation. These results show that the Clp chaperones play a crucial role in both cell division and virulence of L. monocytogenes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ClpC protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0950-382X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
31
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
185-96
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:9987121-Adenosine Triphosphatases,
pubmed-meshheading:9987121-Animals,
pubmed-meshheading:9987121-Bacterial Proteins,
pubmed-meshheading:9987121-Base Sequence,
pubmed-meshheading:9987121-Cell Division,
pubmed-meshheading:9987121-Cloning, Molecular,
pubmed-meshheading:9987121-DNA, Bacterial,
pubmed-meshheading:9987121-Female,
pubmed-meshheading:9987121-Gene Expression Regulation, Bacterial,
pubmed-meshheading:9987121-Heat-Shock Proteins,
pubmed-meshheading:9987121-Listeria monocytogenes,
pubmed-meshheading:9987121-Mice,
pubmed-meshheading:9987121-Mice, Inbred ICR,
pubmed-meshheading:9987121-Molecular Sequence Data,
pubmed-meshheading:9987121-Promoter Regions, Genetic,
pubmed-meshheading:9987121-Transcription, Genetic,
pubmed-meshheading:9987121-Virulence
|
pubmed:year |
1999
|
pubmed:articleTitle |
ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes.
|
pubmed:affiliation |
Inserm U411, Faculté de Médecine Necker, Paris, France. snair@pasteur.fr
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|