复制蛋白A
异三聚体G蛋白
DNA损伤
DNA
DNA复制
生物
SeqA蛋白质结构域
细胞生物学
蛋白质亚单位
DNA结合蛋白
生物化学
真核细胞DNA复制
信号转导
转录因子
G蛋白
基因
作者
Yeyao Wu,Wangmi Fu,Ning Zang,Chun Zhou
出处
期刊:eLife
[eLife Sciences Publications, Ltd.]
日期:2023-09-05
卷期号:12
被引量:5
摘要
The heterotrimeric Replication protein A (RPA) is the ubiquitous eukaryotic single-stranded DNA (ssDNA) binding protein and participates in nearly all aspects of DNA metabolism, especially DNA damage response. The N-terminal OB domain of the RPA70 subunit (RPA70N) is a major protein-protein interaction element for RPA and binds to more than 20 partner proteins. Previous crystallography studies of RPA70N with p53, DNA2 and PrimPol fragments revealed that RPA70N binds to amphipathic peptides that mimic ssDNA. NMR chemical-shift studies also provided valuable information on the interaction of RPA70N residues with target sequences. However, it is still unclear how RPA70N recognizes and distinguishes such a diverse group of target proteins. Here, we present high-resolution crystal structures of RPA70N in complex with peptides from eight DNA damage response proteins. The structures show that, in addition to the ssDNA mimicry mode of interaction, RPA70N employs multiple ways to bind its partners. Our results advance the mechanistic understanding of RPA70N-mediated recruitment of DNA damage response proteins.
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