Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Makhovskaia, O.V.; Kozlov, S.; Botos, I.; Stepnov, A.A.; Andrianova, A.G.; Gushchina, A.E.; Vlodaver, A.; Mel'nikov, E.E.; Rotanova, T.V.; Makhovskaia, O.V; Kozlov, S; Botos, I; Stepnov, A.A; Andrianova, A.G; Gushchina, A.E; Vlodaver, A; Mel&apo; nikov, E.E; Rotanova, T.V

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Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Makhovskaia, O.V.; Kozlov, S.; Botos, I.; Stepnov, A.A.; Andrianova, A.G.; Gushchina, A.E.; Vlodaver, A.; Mel'nikov, E.E.; Rotanova, T.V.

Bioorganicheskaia Khimiia 33(6): 657-660

2007

ISSN/ISBN: 0132-3423

PMID: 18173131

Document Number: 605307

Deletion of the transmembrane domain (TM-domain) of Archaeoglobus flggidus LonB protease (AfLon) was shown to result in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains (alphaP). The deltaTM-AfLonTM-S590A enzyme form, obtained by site-directed mutagenesis of the catalytic Ser residue, is capable of recombination with the alphaP fragment. The mixed oligomers were shown to be proteolytically active, which indicates a crucial role of subunit interactions in the activation of the AfLon proteolytic site. The thermophilic nature of AfLon protease was found to be due to the special features of the enzyme activity regulation, the structure of ATPase domain, and the quaternary structure.