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首页> 外文期刊>Molecular and Cellular Biology >44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.
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44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.

机译：牛乳头瘤病毒的44个氨基酸的E5转化蛋白需要疏水核心和特定的羧基末端氨基酸。

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摘要

The 44-amino-acid E5 protein of bovine papillomavirus type 1 is the shortest known protein with transforming activity. To identify the specific amino acids required for in vitro focus formation in mouse C127 cells, we used oligonucleotide-directed saturation mutagenesis to construct an extensive collection of mutants with missense mutations in the E5 gene. Characterization of mutants with amino acid substitutions in the hydrophobic middle third of the E5 protein indicated that efficient transformation requires a stretch of hydrophobic amino acids but not a specific amino acid sequence in this portion of the protein. Many amino acids in the carboxyl-terminal third of the protein can also undergo substitution without impairment of focus-forming activity, but the amino acids at seven positions, including two cysteine residues that mediate dimer formation, appear essential for efficient transforming activity. These essential amino acids are the most well conserved among related fibropapillomaviruses. The small size of the E5 protein, its lack of similarity to other transforming proteins, and its ability to tolerate many amino acid substitutions implies that it transforms cells via a novel mechanism.
机译：1型牛乳头瘤病毒的44个氨基酸的E5蛋白是已知的最短的具有转化活性的蛋白。为了确定在小鼠C127细胞中体外形成焦点所需的特定氨基酸，我们使用了寡核苷酸定向的饱和诱变来构建E5基因中具有错义突变的大量突变体。在E5蛋白的疏水中间三分之一处具有氨基酸取代的突变体的表征表明，有效的转化需要一段疏水性氨基酸，但在蛋白的这一部分中不需要特定的氨基酸序列。蛋白质羧基末端三分之一的许多氨基酸也可以进行取代，而不会破坏焦点形成活性，但是七个位置的氨基酸（包括两个介导二聚体形成的半胱氨酸残基）似乎对有效的转化活性至关重要。这些必需氨基酸在相关的纤维乳头瘤病毒中是最保守的。 E5蛋白的体积小，缺乏与其他转化蛋白的相似性以及能够耐受许多氨基酸取代的能力暗示着它通过一种新颖的机制转化了细胞。

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