The Helicase Activity of Hyperthermophilic Archaeal MCM is Enhanced at High Temperatures by Lysine Methylation

作者: Yisui Xia , Yanling Niu , Jiamin Cui , Yang Fu , Xiaojiang S. Chen

DOI: 10.3389/FMICB.2015.01247

关键词:

摘要: Lysine methylation and methyltransferases are widespread in the third domain of life, archaea. Nevertheless, effects on archaeal proteins wait to be defined. Here, we report that recombinant sisMCM, an homolog Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 vitro. Mono-methylation these lysine residues occurs coincidently endogenous sisMCM protein purified from hyperthermophilic Sulfolobus islandicus cells as indicated mass spectra. The helicase activity MCM stimulated methylation, particularly at temperatures over 70°C. shows optimal DNA unwinding after heat-treatment between 76 82°C, which correlates well with typical growth Sulfolobus. After half life dramatically extended 80°C. sites located accessible surface, might modulate intra- inter- molecular interactions through changing hydrophobicity surface charge. Furthermore, methylation-mimic mutants show heat resistance comparable MCM. These data provide biochemical evidence posttranslational modifications such may enhance kinetic stability under elevated

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