Linked Life Data

15047485

Source:http://linkedlifedata.com/resource/pubmed/id/15047485

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-3-29
pubmed:abstractText
Proteolysis plays an central role in key metabolic pathways and cellular adaptation to environmental changes. It modulates the activity of regulatory peptides and eliminates misfolded or damaged proteins such as those generated by stress exposure. In eucaryotic cells ATP- dependent proteolysis is carried out by the 26S proteasome whose substrates are identified by ubiquitin tags. Conversely, bacteria possess several tagging systems and different ATP- dependent proteases. Bacterial ATP-dependent proteases carry distinct chaperone-ATPase and peptidase activities, either on the same molecule or on separate subunits. Although unrelated, all ATP-dependent proteases function according to a similar multistep scheme, from the docking of a substrate by the ATPase region to its proteolysis by the peptidase. Major bacterial ATP- dependent proteases include FtsH, Lon, HslUV and the Clp proteases. Clp proteases are multimeric complexes assembled into a structure centered on the proteolytic component ClpP. They are essential for quick adaptation to stress and regulate important developmental processes. Clp-mediated proteolysis is also required for disease progression and virulence of several bacterial pathogens, favoring survival in the host or modulating the activity of genuine virulence factors.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-3898
pubmed:author
pubmed:copyrightInfo
Copyright John Libbey Eurotext 20003.
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[ATP-dependant proteolysis and bacterial pathogenesis].
pubmed:affiliation
Laboratoire de bactériologie-virologie, faculté de médecine de Rennes, 2, avenue Léon Bernard, 35043 Rennes. Olivier.Gaillot@univ-rennes1.fr
pubmed:publicationType
Journal Article, English Abstract, Review