Department of Biophysics, University of Delhi South Campus, New Delhi, India.
Bioinformatics. 2019 Sep 1;35(17):2887-2890. doi: 10.1093/bioinformatics/btz003.
In eukaryotes, palmitoylation drives several essential cellular mechanisms like protein sorting, protein stability and protein-protein interaction. Several amino acids namely Cys, Gly, Ser, Thr and Lys undergo palmitoylation. But very little is known about the amino acid patterns that promote palmitoylation.
We deduced presence of statistically significant amino acids around palmitoylation sites and their association with different palmitoylated residues i.e. Cys, Gly and Ser. The results suggest that palmitoylation, irrespective of its target residue, generally occurs at sites where Cys, Leu, Lys, Arg, Ser and Met are abundant. Furthermore, functional properties of the three types of palmitoylated proteins were compared. We observed similar functional behavior of Cys and Gly palmitoylated proteins but proteins with Ser palmitoylation showed distinctiveness from remaining two. Motif-wise functional conservation was also observed in Cys palmitoylated proteins. We also did functional annotation of predicted human palmitoylome.
Supplementary data are available at Bioinformatics online.
在真核生物中，棕榈酰化驱动着几种重要的细胞机制，如蛋白质分拣、蛋白质稳定性和蛋白质-蛋白质相互作用。几种氨基酸，如 Cys、Gly、Ser、Thr 和 Lys，会发生棕榈酰化。但是，关于促进棕榈酰化的氨基酸模式，我们知之甚少。
我们推断出棕榈酰化位点周围存在统计学意义上显著的氨基酸，以及它们与不同棕榈酰化残基（即 Cys、Gly 和 Ser）的关联。结果表明，无论其靶残基如何，棕榈酰化通常发生在富含 Cys、Leu、Lys、Arg、Ser 和 Met 的位点。此外，我们还比较了三种类型的棕榈酰化蛋白的功能特性。我们观察到 Cys 和 Gly 棕榈酰化蛋白具有相似的功能行为，但 Ser 棕榈酰化蛋白的功能与其余两种明显不同。Cys 棕榈酰化蛋白在基序上也表现出功能保守性。我们还对预测的人类棕榈酰组进行了功能注释。
补充数据可在“Bioinformatics”在线获取。
