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核因子δEF1的鉴定及其对δ1-晶状体蛋白增强子晶状体特异性活性至关重要的结合位点。

Identification of nuclear factor delta EF1 and its binding site essential for lens-specific activity of the delta 1-crystallin enhancer.

作者信息

Funahashi J, Kamachi Y, Goto K, Kondoh H

机构信息

Department of Molecular Biology, School of Science, Nagoya University, Japan.

出版信息

Nucleic Acids Res. 1991 Jul 11;19(13):3543-7. doi: 10.1093/nar/19.13.3543.

Abstract

The lens-specific reglatory element of the delta 1-crystallin enhancer lies within the core segment (Goto et al., (1990) Mol. Cell. Biol. 10, 935-964). The element was allocated within the 55 bp long HN fragment of the core. Block-wise base substitutions were introduced to the 55 bp and their effect on the enhancer activity of the multimers in lens cells was examined. By base sequence alteration of either of the contiguous blocks 5 and 6, with their original sequence of TTGCT and CACCT, respectively, enhancer activity was totally lost. A lens nuclear factor delta EF1 was found which bound specifically to the base sequences defined by the blocks. DNA binding activity very similar to delta EF1 was also found in extracts of tissues other than lens, suggesting that delta EF1 participates in lens-specific regulation through tissue-dependent modification or interaction with other factors.

摘要

δ1-晶体蛋白增强子的晶状体特异性调控元件位于核心片段内(后藤等人,(1990年)《分子与细胞生物学》10卷,935 - 964页)。该元件定位于核心区域55bp长的HN片段内。对这55bp进行了逐块碱基替换,并检测了其对晶状体细胞中多聚体增强子活性的影响。通过改变相邻的5号和6号块的碱基序列(它们原来的序列分别为TTGCT和CACCT),增强子活性完全丧失。发现了一种晶状体核因子δEF1,它能特异性结合由这些块所界定的碱基序列。在晶状体以外的其他组织提取物中也发现了与δEF1非常相似的DNA结合活性,这表明δEF1通过组织依赖性修饰或与其他因子相互作用参与晶状体特异性调控。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c47/328377/1baac3fd140a/nar00093-0070-a.jpg

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