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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.
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 in En | MEDLINE | ID: mdl-37660294
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli Proteins / Protease La Language: En Journal: Cell Rep Year: 2023 Document type: Article Affiliation country: Estados Unidos
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli Proteins / Protease La Language: En Journal: Cell Rep Year: 2023 Document type: Article Affiliation country: Estados Unidos