Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-11-9
pubmed:abstractText
Biogenesis of prokaryote molybdoenzymes is a complex process leading to the insertion of the molybdenum cofactor in the cytoplasm into a folded apoenzyme before transport through the cell membrane. Usually, specific chaperones belonging to the TorD family are required for the maturation of the molybdoenzymes of the dimethyl sulfoxide reductase family. These chaperones play a crucial role during the biogenesis and the incorporation of the molybdenum cofactor by interacting with the core of the apoprotein. Moreover, they are also involved in the protection of the apoproteins by binding to their N-terminal extremity in an early stage of synthesis. Finally, the TorD-like proteins may possess a proofreading activity and they could target their partners to the twin arginine translocation machinery system for cross-membrane transport of prefolded proteins. The roles of these chaperones during the different steps of molybdoenzyme biogenesis are described.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1574-6968
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
297
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Multiple roles of TorD-like chaperones in the biogenesis of molybdoenzymes.
pubmed:affiliation
Laboratoire de Chimie Bactérienne, Centre National de la Recherche Scientifique, Marseille, France.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't