p300和CBP与猿猴病毒40大T抗原的关联。
Association of p300 and CBP with simian virus 40 large T antigen.
作者信息
Eckner R, Ludlow J W, Lill N L, Oldread E, Arany Z, Modjtahedi N, DeCaprio J A, Livingston D M, Morgan J A
机构信息
Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
出版信息
Mol Cell Biol. 1996 Jul;16(7):3454-64. doi: 10.1128/MCB.16.7.3454.
Abstract
p300 and the CREB-binding protein CBP are two large nuclear phosphoproteins that are structurally highly related. Both function, in part, as transcriptional adapters and are targeted by the adenovirus E1A oncoprotein. We show here that p300 and CBP interact with another transforming protein, the simian virus 40 large T antigen (T). This interaction depends on the integrity of a region of T which is critical for its transforming and mitogenic properties and includes its LXCXE Rb-binding motif. T interferes with normal p300 and CBP function on at least two different levels. The presence of T alters the phosphorylation states of both proteins and inhibits their transcriptional activities on certain promoters. Although E1A and T show little sequence similarity, they interact with the same domain of p300 and CBP, suggesting that this region exhibits considerable flexibility in accommodating diverse protein ligands.
摘要
p300和CREB结合蛋白CBP是两种在结构上高度相关的大型核磷蛋白。二者部分功能作为转录衔接子，并且是腺病毒E1A癌蛋白的作用靶点。我们在此表明，p300和CBP与另一种转化蛋白——猿猴病毒40大T抗原（T）相互作用。这种相互作用取决于T的一个区域的完整性，该区域对其转化和促有丝分裂特性至关重要，并且包括其LXCXE Rb结合基序。T至少在两个不同水平上干扰p300和CBP的正常功能。T的存在改变了这两种蛋白的磷酸化状态，并抑制它们在某些启动子上的转录活性。尽管E1A和T几乎没有序列相似性，但它们与p300和CBP的同一结构域相互作用，这表明该区域在容纳不同蛋白质配体方面具有相当大的灵活性。
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