Ahmad Ishtiaq, Hoessli Daniel C, Walker-Nasir Evelyne, Rafik Saleem M, Shakoori Abdul R
Institute of Molecular Sciences and Bioinformatics, Lahore, Pakistan.
Nucleic Acids Res. 2006 Jan 8;34(1):175-84. doi: 10.1093/nar/gkj401. Print 2006.
Phosphorylation and O-GlcNAc modification often induce conformational changes and allow the protein to specifically interact with other proteins. Interplay of phosphorylation and O-GlcNAc modification at the same conserved site may result in the protein undergoing functional switches. We describe that at conserved Ser/Thr residues of human Oct-2, alternative phosphorylation and O-GlcNAc modification (Yin Yang sites) can be predicted by the YinOYang1.2 method. We propose here that alternative phosphorylation and O-GlcNAc modification at Ser191 in the N-terminal region, Ser271 and 274 in the linker region of two POU sub-domains and Thr301 and Ser323 in the POUh subdomain are involved in the differential binding behavior of Oct-2 to the octamer DNA motif. This implies that phosphorylation or O-GlcNAc modification of the same amino acid may result in a different binding capacity of the modified protein. In the C-terminal domain, Ser371, 389 and 394 are additional Yin Yang sites that could be involved in the modulation of Oct-2 binding properties.
磷酸化和O-连接的N-乙酰葡糖胺（O-GlcNAc）修饰常常会引起构象变化，并使蛋白质能够与其他蛋白质发生特异性相互作用。在同一保守位点上，磷酸化与O-GlcNAc修饰之间的相互作用可能会导致蛋白质发生功能转换。我们描述了通过YinOYang1.2方法可以预测人Oct-2保守的丝氨酸/苏氨酸残基上的选择性磷酸化和O-GlcNAc修饰（阴阳位点）。我们在此提出，N端区域的Ser191、两个POU亚结构域连接区域的Ser271和274以及POUh亚结构域中的Thr301和Ser323处的选择性磷酸化和O-GlcNAc修饰，参与了Oct-2与八聚体DNA基序的差异结合行为。这意味着同一氨基酸的磷酸化或O-GlcNAc修饰可能会导致修饰后的蛋白质具有不同的结合能力。在C端结构域中，Ser371、389和394是另外的阴阳位点，可能参与Oct-2结合特性的调节。
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