Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins.
Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins.
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DOI：
10.1099/0022-1317-72-2-411
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发表时间：
1991-02
期刊：
影响因子：
--
通讯作者：
J. Vanslyke;C. A. Franke;D. Hruby
中科院分区：
文献类型：
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作者：
J. Vanslyke;C. A. Franke;D. Hruby
痘苗病毒病毒粒子核心内的三种结构蛋白（4a、4b 和 25K）是病毒感染后期合成的前体多肽（P4a、P4b 和 P25K）的裂解产物。脉冲追踪标记实验表明，核心蛋白的裂解明显落后于前体合成，并且加工需要连续的蛋白质合成。 4b 和 25K 的 N 端序列（而非 4a）是通过对从纯化病毒颗粒中分离的核心蛋白进行微测序确定的。将这些数据与 P4b 和 P25K 的预测氨基酸序列进行比较，揭示了两种蛋白质表面 N 末端侧翼的保守 Ala-Gly-Ala 基序，以及推定裂解位点上游和下游的 P4b 和 P25K 前体之间的一些额外序列相似性。在鸡痘病毒同源蛋白氨基酸序列的同一区域也发现了Ala-Gly-Ala三肽信号。
Three structural proteins (4a, 4b and 25K) located within the virion core of vaccinia virus are cleavage products of precursor polypeptides (P4a, P4b and P25K) synthesized late in viral infection. Pulse-chase labelling experiments revealed that cleavage of the core proteins lags considerably behind precursor synthesis and that processing requires continuous protein synthesis. The N-terminal sequences of 4b and 25K, but not 4a, were determined by microsequencing core proteins isolated from purified virions. Comparison of these data with the predicted amino acid sequence of P4b and P25K revealed a conserved Ala-Gly-Ala motif flanking the apparent N termini of both proteins, as well as several additional sequence similarities between the P4b and P25K precursors both upstream and downstream of the putative cleavage site. The Ala-Gly-Ala tripeptide signal was also found in the same region of the amino acid sequences of the homologous proteins of fowlpox virus.