Role of α-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli

Андрианова, А. Г.; Kudzhaev, A. M.; Serova, O. V.; Дергоусова, Н. И.; Rotanova, T. V.

doi:10.1134/s106816201406003x

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…In terms of enzymatic properties, the newly isolated Bs LonBA-H6 protease is radically different from the “classical” Ec LonA. The latter enzyme, which also bore a C-terminal hexahistidine tag, was shown to hydrolyze ATP effectively, and, in the presence of a protein substrate, the ATPase activity increased significantly [ 42 , 43 ]. However, Bs LonBA-H6 does not show the ability to hydrolyze ATP either in the absence or in the presence of a substrate protein.…”

Section: Resultsmentioning

confidence: 99%

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases

Gustchina

Андрианова

et al. 2022

IJMS

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ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are single-chain, multidomain proteins containing an ATPase and protease domains, with different additional elements present in each subfamily. LonA and LonC proteases are soluble cytoplasmic enzymes, whereas LonBs are membrane-bound. Based on an analysis of the available sequences of Lon proteases, we identified a number of enzymes currently assigned to the LonB subfamily that, although presumably membrane-bound, include structural features more similar to their counterparts in the LonA subfamily. This observation was confirmed by the crystal structure of the proteolytic domain of the enzyme previously assigned as Bacillus subtilis LonB, combined with the modeled structure of its ATPase domain. Several structural features present in both domains differ from their counterparts in either LonA or LonB subfamilies. We thus postulate that this enzyme is the founding member of a newly identified LonBA subfamily, so far found only in the gene sequences of firmicutes.

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Section: Resultsmentioning

confidence: 99%

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases

Gustchina

Андрианова

et al. 2022

IJMS

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“…The recombinant Ec-Lon protease used in the study, which contained an additional C-terminal octapeptide bearing a hexahistidine fragment (Lon-H 6 ), had been produced and characterized previously [ 15 ]. The recombinant deletion form Lon-dHI(CC), without the inserted HI(CC) domain (residues Glu124–Asn304, Fig.…”

Section: Resultsmentioning

confidence: 99%

“…A recombinant form of Ec-Lon containing a hexahistidine fragment (in LEHHHHHH octapeptide) at the C-terminus of the protein (Lon-H 6 ) was prepared according to the previously described procedure [ 15 ].…”

Section: Methodsmentioning

confidence: 99%

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Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function

et al. 2017

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Multidomain ATP-dependent Lon protease of E. coli (Ec-Lon) is one of the key enzymes of the quality control system of the cellular proteome. A recombinant form of Ec-Lon with deletion of the inserted characteristic α-helical HI(CC) domain (Lon-dHI(CC)) has been prepared and investigated to understand the role of this domain. A comparative study of the ATPase, proteolytic, and peptidase activities of the intact Lon protease and Lon-dHI(CC) has been carried out. The ability of the enzymes to undergo autolysis and their ability to bind DNA have been studied as well. It has been shown that the HI(CC) domain of Ec-Lon protease is required for the formation of a functionally active enzyme structure and for the implementation of protein-protein interactions.

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“…This protease also exhibited cleavage activity against fluorogenic peptides in the presence of ATP and Mg 2+ . Lon from E. coli [ 21 ] exhibits maximal efficiency when ATP is bound and hydrolyzed in the presence of Mg 2+ . However, fluorogenic peptide degradation was also shown to occur in the presence of nonhydrolyzable AMP-PNP.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the ATP-Dependent Lon-Like Protease inMethanobrevibacter smithii

Pei

Yan

Jiang

2016

Archaea

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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.

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Role of α-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli

Cited by 7 publications

References 23 publications

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases

Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function

Characterization of the ATP-Dependent Lon-Like Protease inMethanobrevibacter smithii

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