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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F14%3A00436201" target="_blank" >RIV/61388971:_____/14:00436201 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1111/febs.12740" target="_blank" >http://dx.doi.org/10.1111/febs.12740</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.12740" target="_blank" >10.1111/febs.12740</a>

Result language

angličtina

Original language name

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

Original language description

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 -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 -casein-stimulated activity. The loop containing Gly8

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

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Volume of the periodical

281

Issue of the periodical within the volume

7

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

1784-1797

UT code for WoS article

000333676000007

EID of the result in the Scopus database

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