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首页> 外文期刊>Biochemistry >Inhibition of Protein Interactions with the beta_2 Sliding Clamp of Escherichia coli DNA Polymerase III by Peptides from beta_2-Binding Proteins
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Inhibition of Protein Interactions with the beta_2 Sliding Clamp of Escherichia coli DNA Polymerase III by Peptides from beta_2-Binding Proteins

机译:β_2结合蛋白的肽对大肠杆菌DNA聚合酶III的beta_2滑动夹的蛋白质相互作用的抑制作用

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摘要

The sliding clamp of the Escherichia coli replisome is now understood to interact with many proteins involved in DNA synthesis and repair.A universal interaction motif is proposed to be one mechanism by which those proteins bind the E.coli sliding clamp,a homodimer of the beta subunit,at a single site on the dimer.The numerous beta_2-binding proteins have various versions of the consensus interaction motif,including a related hexameric sequence.To determine if the variants of the motif could contribute to the competition of the beta-binding proteins for the beta_2 site,synthetic peptides derived from the putative beta_2-binding motifs were assessed for their abilities to inhibit protein-beta_2 interactions,to bind directly to beta_2,and to inhibit DNA synthesis in vitro.A hierarchy emerged,which was consistent with sequence similarity to the pentameric consensus motif,QL(S/D)LF,and peptides containing proposed hexameric motifs were shown to have activities comparable to those containing the consensus sequence.The hierarchy of peptide binding may be indicative of a competitive hierarchy for the binding of proteins to beta_2 in various stages or circumstances of DNA replication and repair.
机译:现已理解,大肠杆菌复制体的滑动夹具可与许多参与DNA合成和修复的蛋白质相互作用。普遍的相互作用基序被认为是这些蛋白质结合E.coli滑动夹具(β的同二聚体)的一种机制。大量的beta_2结合蛋白具有多种版本的共有相互作用基序,包括相关的六聚体序列。确定该基序的变体是否有助于促进β结合蛋白的竞争对于beta_2位点,评估了推定的beta_2结合基序衍生的合成肽抑制蛋白质-beta_2相互作用,直接与beta_2结合以及体外抑制DNA合成的能力。出现了层次结构,该序列与序列一致与五聚体共有基序QL(S / D)LF具有相似性,并且含有拟议六聚体基序的肽具有与含五聚体共有基序相当的活性肽结合的层次可以指示在DNA复制和修复的不同阶段或情况下蛋白质与β_2结合的竞争层次。

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