characterization of the atp-dependent lon-like protease in methanobrevibacter smithii
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ID: 245564
2016
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Abstract
The Lon protease is highly evolutionarily conserved. However, little is known about Lon in the context of gut microbial communities. A gene encoding a Lon-like protease (Lon-like-Ms) was identified and characterized from Methanobrevibacter smithii, the predominant archaeon in the human gut ecosystem. Phylogenetic and sequence analyses showed that Lon-like-Ms and its homologs are newly identified members of the Lon family. A recombinant form of the enzyme was purified by affinity chromatography, and its catalytic properties were examined. Recombinant Lon-like-Ms exhibited ATPase activity and cleavage activity toward fluorogenic peptides and casein. The peptidase activity of Lon-like-Ms relied strictly on Mg2+ (or other divalent cations) and ATP. These results highlight a new type of Lon-like protease that differs from its bacterial counterpart.
| Reference Key |
pei2016archaeacharacterization
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|---|---|
| Authors | ;Jihua Pei;Jianfang Yan;Yi Jiang |
| Journal | annals of nuclear energy |
| Year | 2016 |
| DOI |
10.1155/2016/5759765
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| URL | |
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