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首页> 外文期刊>Molecular and Cellular Biology >Acquisition of NFKB1-selective DNA binding by substitution of four amino acid residues from NFKB1 into RelA.
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Acquisition of NFKB1-selective DNA binding by substitution of four amino acid residues from NFKB1 into RelA.

机译：通过将NFKB1中的四个氨基酸残基置换为RelA，获得NFKB1选择性DNA结合。

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The subunits of NF-kappa B, NFKB1 (formerly p50) and RelA (formerly p65), belong to a growing family of transcription factors that share extensive similarity to the c-rel proto-oncogene product. The homology extends over a highly conserved stretch of approximately 300 amino acids termed the Rel homology domain (RHD). This region has been shown to be involved in both multimerization (homo- and heterodimerization) and DNA binding. It is now generally accepted that homodimers of either subunit are capable of binding DNA that contains a kappa B site originally identified in the immunoglobulin enhancer. Recent studies have demonstrated that the individual subunits of the NF-kappa B transcription factor complex can be distinguished by their ability to bind distinct DNA sequence motifs. By using NFKB1 and RelA subunit fusion proteins, different regions within the RHD were found to confer DNA-binding and multimerization functions. A fusion protein that contains 34 N-terminal amino acids of NFKB1 and 264 amino acids of RelA displayed preferential binding to an NFKB1-selective DNA motif while dimerizing with the characteristics of RelA. Within the NFKB1 portion of this fusion protein, a single amino acid change of His to Arg altered the DNA-binding specificity to favor interaction with the RelA-selective DNA motif. Furthermore, substitution of four amino acids from NFKB1 into RelA was able to alter the DNA-binding specificity of the RelA protein to favor interaction with the NFKB1-selective site. Taken together, these findings demonstrate the presence of a distinct subdomain within the RHD involved in conferring the DNA-binding specificity of the Rel family of proteins.
机译：NF-κB的亚基，NFKB1（以前为p50）和RelA（以前为p65）属于与c-rel原癌基因产物有着广泛相似性的转录因子家族。同源性延伸到被称为Rel同源性结构域（RHD）的大约300个氨基酸的高度保守的片段上。已显示该区域参与多聚化（同二聚和异二聚化）和DNA结合。现在普遍接受的是，任何一个亚基的同二聚体都能够结合含有最初在免疫球蛋白增强子中识别的κB位点的DNA。最近的研究表明，NF-κB转录因子复合物的各个亚基可以通过它们结合不同DNA序列基序的能力来区分。通过使用NFKB1和RelA亚基融合蛋白，发现RHD中的不同区域具有DNA结合和多聚化功能。包含NFKB1的34个N末端氨基酸和RelA的264个氨基酸的融合蛋白显示出优先结合NFKB1选择性DNA基序，同时具有RelA的特征二聚化。在该融合蛋白的NFKB1部分内，His变为Arg的单个氨基酸改变改变了DNA结合特异性，从而促进了与RelA选择性DNA图案的相互作用。此外，将NFKB1中的四个氨基酸替换为RelA能够改变RelA蛋白的DNA结合特异性，从而促进与NFKB1选择位点的相互作用。综上所述，这些发现证明RHD内存在一个独特的亚结构域，该亚结构域涉及赋予Rel蛋白家族的DNA结合特异性。

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