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Identification of the Dimer Exchange Interface of the Bacterial DNA Damage Response Protein UmuD

机译：鉴定细菌DNA损伤反应蛋白udud的二聚体交换界面

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摘要

The Escherichia coli SOS response, an induced DNA damage response pathway, confers survival on bacterial cells by providing accurate repair mechanisms as well as the potentially mutagenic pathway translesion synthesis (TLS). The umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response. Full-length UmuD is expressed as a homodimer of 139-amino-acid subunits, which eventually,cleaves its N-terminal 24 amino acids to form UmuD'. The cleavage product UmuD' and UmuC form the Y-family polymerase DNA Pol V (UmuD'C-2) capable of performing TLS. UmuD and UninD' exist as homodimers, but their subunits can readily exchange to form UmuDD' heterodimers preferentially. Heterodimer formation is an essential step in the degradation pathway of UmuD'. The recognition sequence for C1pXP protease is located within the first 24 amino acids of full-length UxnuD, and the partner of full-length UmuD, whether UmuD or UmutY, is degraded by C1pXP. To better understand the mechanism by which UmuD subunits exchange, we measured the kinetics of exchange of a number of fluorescently labeled single-cysteine UmuD variants as detected by Forster resonance energy transfer. Labeling sites near the dimer interface correlate with increased rates of exchange, indicating that weakening the dimer interface facilitates exchange, whereas labeling sites on the exterior decrease the rate of exchange. In most but not all cases, homodimer and heterodimer exchange exhibit similar rates, indicating that somewhat different molecular surfaces mediate homodimer exchange and heterodimer formation.
机译：大肠杆菌SOS反应是一种诱导的DNA损伤响应途径，通过提供准确的修复机制以及潜在的诱变途径转换合成（TLS）来赋予细菌细胞的存活。在DNA损伤后umud基因产物在SOS反应的非培养和致突变性方面发挥作用后上调。全长umud表示为139-氨基酸亚基的同态二聚体，最终切割其N-末端24氨基酸以形成umud'。切割产物umud'和UMUC形成能够进行TLS的Y家族聚合酶DNA POL V（UMUD'C-2）。 umud和unind'存在作为同源体，但它们的亚基可以易于交换以优选地形成umudd的异二聚体。异二聚体形成是umud'的降解途径的重要步骤。 C1PXP蛋白酶的识别序列位于全长UxNUD的前24个氨基酸内，并且全长umud的伴侣是由C1PXP降解的。为了更好地理解umud亚基交换的机制，我们测量了通过福尔斯特共振能量转移检测到的许多荧光标记的单半胱氨酸udiants的交换动力学。 Dimer接口附近的标记站点与更高的交换率相关，表明Dimer接口促进交换的弱化，而在外部的标记网站降低了交换速率。在大多数情况下，但不是所有病例，同源过二聚体和异二聚体交换表现出类似的速率，表明有些不同的分子表面介导同型二聚体交换和异二聚体形成。

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  • 来源
    《Biochemistry》 |2017年第36期|共13页
  • 作者

    Murison David A.; Timson Rebecca C.; Koleva Bilyana N.; Ordazzo Michael; Beuning Penny J.;

  • 作者单位

    Northeastern Univ Dept Chem &

    Chem Biol 360 Huntington Ave 102 Hurtig Hall Boston MA 02115 USA;

    Northeastern Univ Dept Chem &

    Chem Biol 360 Huntington Ave 102 Hurtig Hall Boston MA 02115 USA;

    Northeastern Univ Dept Chem &

    Chem Biol 360 Huntington Ave 102 Hurtig Hall Boston MA 02115 USA;

    Northeastern Univ Dept Chem &

    Chem Biol 360 Huntington Ave 102 Hurtig Hall Boston MA 02115 USA;

    Northeastern Univ Dept Chem &

    Chem Biol 360 Huntington Ave 102 Hurtig Hall Boston MA 02115 USA;

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  • 正文语种 eng
  • 中图分类 生物化学;
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