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 |
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| Authors: | O V Makhovskaya S Kozlov I Botos A A Stepnov A G Andrianova A E Gushchina A Wlodawer E E Mel’nikov T V Rotanova |
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| Institution: | (1) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow, 117997, Russia;(2) Cancer and Developmental Biology Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702-1201, USA;(3) Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA;(4) Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA |
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| Abstract: | Deletion of the transmembrane domain (TM-domain) of Archaeoglobus fulgidus LonB protease (Archaeoglobus fulgidus (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 α-helical and proteolytic domains (αP). The ΔTM-AfLon-S509A enzyme form, obtained by site-directed mutagenesis of the catalytic Ser residue, is capable of recombination with the αP 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. |
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| Keywords: | Archaeoglobus fulgidus Lon protease proteolytic activity subunit interactions transmembrane domain |
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