SPECIFICITY OF DNAK PEPTIDE BINDING
SPECIFICITY OF DNAK PEPTIDE BINDING
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DOI：
10.1006/jmbi.1994.1043
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发表时间：
1994-01-21
影响因子：
5.6
通讯作者：
GOTTESMAN, ME
中科院分区：
文献类型：
--
作者：
GRAGEROV, A;LI, Z;GOTTESMAN, ME
DnaK底物结合的序列特异性已经使用肽展示文库进行了研究。基于在该选择中出现的氨基酸模式，合成短肽用于直接测量DnaK亲和力。结果表明，富含疏水残基的肽段是DnaK的优先底物，带负电荷的肽段亲和力较差，DnaK的C端结构域与肽段结合。肽解离研究表明，结合肽从C-末端片段和DnaK以相同的速率释放。ATP刺激肽从DnaK解离，但不刺激肽从C-末端片段解离。
The sequence specificity of DnaK substrate binding has been studied using a peptide display library. Based on the amino acid patterns that appeared in this selection, short peptides were synthesized for direct measurements of DnaK affinity. The results show that peptides enriched in internal hydrophobic residues are preferential DnaK substrates, and negatively charged peptides have poor affinity.The isolated C-terminal domain of DnaK binds peptides. Peptide dissociation studies indicate that bound peptides are released from the C-terminal fragment and from DnaK at identical rates. ATP stimulates peptide dissociation from DnaK but not from the C-terminal fragment.