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Literature summary for 3.4.21.53 extracted from

  • Liao, J.H.; Lin, Y.C.; Hsu, J.; Lee, A.Y.; Chen, T.A.; Hsu, C.H.; Chir, J.L.; Hua, K.F.; Wu, T.H.; Hong, L.J.; Yen, P.W.; Chiou, A.; Wu, S.H.
    Binding and cleavage of E. coli HUbeta by the E. coli Lon protease (2010), Biophys. J., 98, 129-137.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-binding protein HUbeta + H2O Lon binds to both histone-like proteins HUalpha and HUbeta, but selectively degrades only HUbeta in the presence of ATP. Preferred cleavage site is the A20-A21, followed in preference by L36-K37. Degradation of substrate mutants A20D and A20Q is more slowly. Mechanism follows at least three stages: binding of Lon with the HU protein, hydrolysis of ATP by Lon to provide energy to loosen the binding to the HU protein and to allow an induced-fit conformational change, and specific cleavage of only HUbeta Escherichia coli ?
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