Chaperone protection of immature molybdoenzyme during molybdenum cofactor limitation.

Abstract

Maturation of molybdoenzyme TorA involves chaperone TorD. This study shows that TorD is also required to protect apoTorA against proteolysis when the molybdenum cofactor is limiting in Escherichia coli. The absence of TorD leads to a complete loss of apoTorA during molybdenum cofactor deficiency whereas the presence of TorD maintains a significant amount of apoTorA that can be matured when the molybdenum cofactor becomes available.

• Authors: Olivier Genest, Farida Seduk, Laurence Théraulaz, Vincent Méjean, Chantal Iobbi-Nivol
• Journal: FEMS microbiology letters (FEMS Microbiol Lett) Vol. 265 Issue 1 Pg. 51-5 (Dec 2006) ISSN: 0378-1097 [Print] England
• PMID: 17107419 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Apoenzymes
• Coenzymes
• Escherichia coli Proteins
• Metalloproteins
• Molecular Chaperones
• Molybdenum Cofactors
• Pteridines
• TorD protein, E coli
• molybdenum cofactor
• Oxidoreductases, N-Demethylating
• trimethylamine dehydrogenase

Topics

• Apoenzymes (metabolism)
• Coenzymes (metabolism)
• Escherichia coli (enzymology, genetics)
• Escherichia coli Proteins (metabolism)
• Metalloproteins (metabolism)
• Molecular Chaperones (metabolism)
• Molybdenum Cofactors
• Oxidoreductases, N-Demethylating (metabolism)
• Pteridines (metabolism)