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噬菌体T4的裂解蛋白T

Lysis protein T of bacteriophage T4.

作者信息

Lu M J, Henning U

机构信息

Max-Planck-Institut für Biologie, Tübingen, FRG.

出版信息

Mol Gen Genet. 1992 Nov;235(2-3):253-8. doi: 10.1007/BF00279368.

Abstract

Lysis protein T of phage T4 is required to allow the phage's lysozyme to reach the murein layer of the cell envelope and cause lysis. Using fusions of the cloned gene t with that of the Escherichia coli alkaline phosphatase or a fragment of the gene for the outer membrane protein OmpA, it was possible to identify T as an integral protein of the plasma membrane. The protein was present in the membrane as a homooligomer and was active at very low cellular concentrations. Expression of the cloned gene t was lethal without causing gross leakiness of the membrane. The functional equivalent of T in phage lambda is protein S. An amber mutant of gene S can be complemented by gene t, although neither protein R of lambda (the functional equivalent of T4 lysozyme) nor S possess any sequence similarity with their T4 counterparts. The murein-degrading enzymes (including that of phage P22) have in common a relatively small size (molecular masses of ca. 18,000) and a rather basic nature not exhibited by other E. coli cystosolic proteins. The results suggest that T acts as a pore that is specific for this type of enzyme.

摘要

噬菌体T4的裂解蛋白T是使噬菌体的溶菌酶能够到达细胞包膜的胞壁质层并引起裂解所必需的。利用克隆的基因t与大肠杆菌碱性磷酸酶的基因或外膜蛋白OmpA的基因片段的融合,有可能将T鉴定为质膜的整合蛋白。该蛋白以同型寡聚体形式存在于膜中,并且在非常低的细胞浓度下具有活性。克隆基因t的表达是致死性的,但不会导致膜出现明显渗漏。噬菌体λ中T的功能等效物是蛋白S。基因S的琥珀突变体可以由基因t互补,尽管λ的蛋白R(T4溶菌酶的功能等效物)和S与它们在T4中的对应物都没有任何序列相似性。胞壁质降解酶(包括噬菌体P22的酶)共同具有相对较小的尺寸(分子量约为18,000)和其他大肠杆菌胞质蛋白所不具有的相当碱性的性质。结果表明,T作为一种对这类酶具有特异性的孔道发挥作用。

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