The Amino Acid Composition of Quadruplex Binding Proteins Reveals a Shared Motif and Predicts New Potential Quadruplex Interactors.

The Amino Acid Composition of Quadruplex Binding Proteins Reveals a Shared Motif and Predicts New Potential Quadruplex Interactors.
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DOI:
10.3390/molecules23092341
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发表时间:
2018-09-13
期刊:
Molecules (Basel, Switzerland)
影响因子:
--
通讯作者:
Pečinka P
Pečinka P
中科院分区:
其他
文献类型:
--
作者:
Brázda V;Červeň J;Bartas M;Mikysková N;Coufal J;Pečinka P

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局部DNA结构在调节基本细胞过程中的重要性是一个新兴的研究领域。在局部非B DNA结构中,G-四链体可能是迄今为止最好表征的,并且它们的存在已在许多基因组中得到证实,包括人类的基因组。G-四链体被许多调节蛋白选择性地结合。在本文中,我们分析了所有77个描述的G-四链体结合蛋白的智人的氨基酸组成。我们与所有人类蛋白质和特定蛋白质亚群(例如,所有核酸结合)显示了四链体结合蛋白的独特特征,具有显著的甘氨酸(G)和精氨酸(R)富集。聚类分析与bootstrap resstrom显示特定的四链体结合蛋白的氨基酸组成的相似性和差异。有趣的是,我们发现所有表征的G-四链体结合蛋白共有一个20个氨基酸长的基序/结构域(RGRGR GRGGG SGGSG GRGRG),其类似于先前描述的FRM 1 G-四链体结合蛋白的富RG结构域(RRGDG RRRGG GGRGQ GGRGR GGGFKG)。基于这个蛋白质指纹,我们预测了一组新的潜在的G-四链体结合蛋白共享这个有趣的域丰富的甘氨酸和精氨酸残基。
The importance of local DNA structures in the regulation of basic cellular processes is an emerging field of research. Amongst local non-B DNA structures, G-quadruplexes are perhaps the most well-characterized to date, and their presence has been demonstrated in many genomes, including that of humans. G-quadruplexes are selectively bound by many regulatory proteins. In this paper, we have analyzed the amino acid composition of all seventy-seven described G-quadruplex binding proteins of Homo sapiens. Our comparison with amino acid frequencies in all human proteins and specific protein subsets (e.g., all nucleic acid binding) revealed unique features of quadruplex binding proteins, with prominent enrichment for glycine (G) and arginine (R). Cluster analysis with bootstrap resampling shows similarities and differences in amino acid composition of particular quadruplex binding proteins. Interestingly, we found that all characterized G-quadruplex binding proteins share a 20 amino acid long motif/domain (RGRGR GRGGG SGGSG GRGRG) which is similar to the previously described RG-rich domain (RRGDG RRRGG GGRGQ GGRGR GGGFKG) of the FRM1 G-quadruplex binding protein. Based on this protein fingerprint, we have predicted a new set of potential G-quadruplex binding proteins sharing this interesting domain rich in glycine and arginine residues.
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