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

A M Kudzhaev; A G Andrianova; E S Dubovtseva; O V Serova; T V Rotanova

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

Acta Naturae. 2017 Apr-Jun;9(2):75-81.

Authors

A M Kudzhaev¹, A G Andrianova¹, E S Dubovtseva¹, O V Serova¹, T V Rotanova¹

Affiliation

¹ Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str., 16/10, Moscow, 117997, Russia.

PMID: 28740729
PMCID: PMC5509003

Abstract

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.

Keywords: AAA+ proteins; ATP-dependent proteolysis; DNA binding; LonA proteases; inserted α-helical domain.