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噬菌体M13原衣壳蛋白以环状结构插入质膜。

Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure.

作者信息

Kuhn A

机构信息

Microbiology Department, University of Basel, Switzerland.

出版信息

Science. 1987 Dec 4;238(4832):1413-5. doi: 10.1126/science.3317833.

Abstract

The major coat protein of bacteriophage M13 is synthesized as a precursor, the procoat, with a typical leader (signal) sequence of 23 residues at its NH2-terminus. A fusion protein that contains the NH2-terminal 141 residues of cytoplasmic ribulokinase and all but the first ten residues of M13 procoat was made. The fusion protein inserts into the plasma membrane of Escherichia coli and is processed by leader peptidase to give rise to a leader peptide of 155 residues and the mature coat protein of 50 residues. The NH2-terminus of the leader peptide remains in the cytoplasm and is protected from protease added to the medium outside of the cell. This indicates that M13 procoat inserts into the membrane as a loop structure and that the NH2-terminus of a leader peptide remains within the cytoplasm during membrane insertion.

摘要

噬菌体M13的主要外壳蛋白以前体形式合成,即前衣壳蛋白,在其NH2末端有一段典型的由23个残基组成的前导(信号)序列。构建了一种融合蛋白,它包含细胞质核酮糖激酶的NH2末端141个残基以及除M13前衣壳蛋白前十个残基之外的所有残基。该融合蛋白插入大肠杆菌的质膜,并被前导肽酶加工,产生一个由155个残基组成的前导肽和一个由50个残基组成的成熟外壳蛋白。前导肽的NH2末端保留在细胞质中,并受到添加到细胞外培养基中的蛋白酶的保护。这表明M13前衣壳蛋白以环结构插入膜中,并且在前导肽插入膜的过程中,其NH2末端保留在细胞质内。

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