A FACTOR PREVENTING MAJOR HEAD PROTEIN OF BACTERIOPHAGE T4 FROM RANDOM AGGREGATION
A FACTOR PREVENTING MAJOR HEAD PROTEIN OF BACTERIOPHAGE T4 FROM RANDOM AGGREGATION
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DOI：
10.1016/0022-2836(70)90402-x
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发表时间：
1970-01-01
影响因子：
5.6
通讯作者：
GUJERKEL, G
中科院分区：
文献类型：
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作者：
LAEMMLI, UK;BEGUIN, F;GUJERKEL, G
噬菌体T4基因31（P31）的产物是噬菌体衣壳及其相关结构形成所必需的。在没有活性P31的情况下，产物P23（噬菌体衣壳的主要组分）聚集成“团块”，其与细胞包膜一起沉淀。用基因31中的ts-突变体进行的温度变化实验表明，P23聚集体可以被活化的P31溶解，并且溶解的P23是正常的，因为它可以用于掺入到活性噬菌体中。P31基因的两个不同突变体产生两种不同的温度敏感蛋白。如果在限制性温度下产生，则不可逆地失活;但是当在允许温度下合成时，它变得热稳定，并且在限制性温度下保持功能。另一个是可逆的温度影响，激活后转移到允许的温度和失活，如果限制温度成立。
The product of gene 31 (P31) of bacteriophage T4 is required for the formation of the phage capsid and its related structures. In the absence of active P31, product P23, the major component of the phage capsid, aggregates into “lumps” which sediment with the cell envelope. Temperature-shift experiments withts-mutants in gene 31 demonstrate that the P23 aggregates can be dissolved by activated P31 and the dissolved P23 is normal, in that it can be used for incorporation into active phage. It is possible that P31 acts catalytically.Two differentts-mutants in gene 31 produce two different temperature-sensitive proteins. One is irreversibly inactivated if produced at the restrictive temperature; but when synthesized at the permissive temperature, it becomes heat stable and remains functional at the restrictive temperature. The other is reversibly affected by temperature, activated following shift to permissive temperature and inactivated if restrictive temperature is established.