Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.

Kasal, Meghann R; Kotamarthi, Hema Chandra; Johnson, Madeline M; Stephens, Hannah M; Lang, Matthew J; Sauer, Robert T; Baker, Tania A

Kasal, Meghann R; Kotamarthi, Hema Chandra; Johnson, Madeline M; Stephens, Hannah M; Lang, Matthew J; Sauer, Robert T; Baker, Tania A.

Affiliation

Kasal MR; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Kotamarthi HC; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Johnson MM; Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235, USA.
Stephens HM; Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235, USA.
Lang MJ; Department of Chemical and Biomolecular Engineering, Vanderbilt University, Nashville, TN 37235, USA.
Sauer RT; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Baker TA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: tabaker@mit.edu.

Cell Rep ; 42(9): 113061, 2023 09 26.

Article de En | MEDLINE | ID: mdl-37660294

Sujet(s)
Mots clés

AAA+ enzyme processivity; AAA+ motors; AAA+ unfoldase translocation step size; CP: Molecular biology; protein degradation; single-molecule optical trapping

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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Protéines Escherichia coli / Protease La Langue: En Journal: Cell Rep Année: 2023 Type de document: Article Pays d'affiliation: États-Unis d'Amérique Pays de publication: États-Unis d'Amérique

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