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Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ambro, Lubos Pevala, Vladimír Ondrovicová, Gabriela Bellová, Jana Kunová, Nina Kutejová, Eva Bauer, Jacob
Description	Country affiliation: Slovakia Author Affiliation: Ambro L ( Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Slovakia.)
Abstract	UNLABELLED: Lon, also called protease La, is an ATP-dependent protease present in all kingdoms of life. It is involved in protein quality control and several regulatory processes. Eukaryotic Lon possesses three domains, an N-terminal domain, an ATPase domain and a proteolytic domain. It requires ATP hydrolysis to digest larger, intact proteins, but can cleave small, fluorogenic peptides such as Glu-Ala-Ala-Phe-MNA by only binding, but not hydrolyzing, ATP. Both ATPase and peptidase activities can be stimulated by the binding of a larger protein substrate, such as ß-casein. To better understand its mechanism of action, we have prepared several point mutants of four conserved residues of human Lon (G893A, G893P, G894A, G894P, G894S, G893A-G894A, G893P-G894A, G893A-G894P, T880V, W770A, W770P) and studied their ATPase, protease and peptidase activities. Our results show that mutations to Gly894 enhance its basal ATPase activity but do not change its ß-casein-stimulated activity. The loop containing Gly893 and Gly894, which flanks Lon's proteolytic active site, therefore appears to be involved in the conformational change that occurs upon substrate binding. Furthermore, mutations to Trp770 have the same general effects on the ATPase activity as mutations to Gly893, indicating that Trp770 is involved in ATPase stimulation. We have also established that this loop does not need to move in order to cleave small, fluorogenic peptides, but does move during the digestion of ß-casein. Finally, we also noted that Lon's ability to digest small peptides can be inhibited by moderate ATP concentrations. DATABASE: Lon (Endopeptidase La), EC 4.4.21.53 STRUCTURED DIGITAL ABSTRACT: â¢ hLonP cleaves beta casein by protease assay (1, 2, 3, 4, 5, 6) â¢ hLon and hLon bind by cross-linking study (View interaction).
File Format	HTM / HTML
ISSN	1742464X
Issue Number	7
Volume Number	281
e-ISSN	17424658
Journal	FEBS Journal
Language	English
Publisher	Wiley (on behalf of the Federation of European Biochemical Societies)
Publisher Date	2014-04-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Adenosine Triphosphate Metabolism Catalytic Domain Mutation Protease La Amino Acid Sequence Caseins Enzyme Activation Humans Molecular Sequence Data Chemistry Genetics Protein Binding Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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