Structural basis for allosteric PARP-1 retention on DNA breaks
نویسندگان
چکیده
منابع مشابه
Fluorescent sensors of PARP-1 structural dynamics and allosteric regulation in response to DNA damage
Poly(ADP-ribose) (PAR) is a posttranslational modification predominantly synthesized by PAR polymerase-1 (PARP-1) in genome maintenance. PARP-1 detects DNA damage, and damage detection is coupled to a massive increase PAR production, primarily attached to PARP-1 (automodification). Automodified PARP-1 then recruits repair factors to DNA damage sites. PARP-1 automodification eventually leads to ...
متن کاملPARP-2 and PARP-3 are selectively activated by 5′ phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1
PARP-1, PARP-2 and PARP-3 are DNA-dependent PARPs that localize to DNA damage, synthesize poly(ADP-ribose) (PAR) covalently attached to target proteins including themselves, and thereby recruit repair factors to DNA breaks to increase repair efficiency. PARP-1, PARP-2 and PARP-3 have in common two C-terminal domains-Trp-Gly-Arg (WGR) and catalytic (CAT). In contrast, the N-terminal region (NTR)...
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Poly-ADP ribose polymerase 1 (PARP-1) is a protein well described as a sensor for single strand DNA breaks (SSB) [1]. After its activation a localized poly(ADPribosyl)ation of proteins near the DNA breaks is initiated, which is necessary for efficient binding of other repair proteins like XRCC1. The aprataxin protein has interaction domains for both SSB-repair proteins such as PARP1 and XRCC1 a...
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Poly(ADP-ribose)polymerase 1 (PARP-1) recognizes DNA strand interruptions in vivo and triggers its own modification as well as that of other proteins by the sequential addition of ADP-ribose to form polymers. This modification causes a release of PARP-1 from DNA ends and initiates a variety of responses including DNA repair. While PARP-1 has been firmly implicated in base excision and single st...
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when the bacterial environment contains no lactose (Al-berts et al., 2002; Berg et al., 2002). The repressor functions as a dimer of two " hand " domains (Figure 1D). loop is critical for the lac operon repression (Matthews, 1992). The primary roles of CAP and LR are the opposite of Summary each other, yet the two proteins bind to DNA cooperatively (Hudson and Fried, 1990; Lewis et al., 1996). ...
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ژورنال
عنوان ژورنال: Science
سال: 2020
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.aax6367