PROCESSING OF TCP PILIN BY TCPJ TYPIFIES A COMMON STEP INTRINSIC TO A NEWLY RECOGNIZED PATHWAY OF EXTRACELLULAR PROTEIN SECRETION BY GRAM-NEGATIVE BACTERIA
PROCESSING OF TCP PILIN BY TCPJ TYPIFIES A COMMON STEP INTRINSIC TO A NEWLY RECOGNIZED PATHWAY OF EXTRACELLULAR PROTEIN SECRETION BY GRAM-NEGATIVE BACTERIA
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DOI：
10.1101/gad.5.10.1834
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发表时间：
1991-10-01
影响因子：
10.5
通讯作者：
TAYLOR, RK
中科院分区：
文献类型：
--
作者：
KAUFMAN, MR;SEYER, JM;TAYLOR, RK
霍乱弧菌毒素共调节菌毛（TCP）的生物发生需要至少7个辅助蛋白的活性。 我们证明，这一途径的一部分涉及一个新的加工步骤，其中亲水性前导肽被蛋白水解去除TcpA的基因产物，其特征在于在本报告中，TcpJ，以产生成熟的，出口能力形式的菌毛蛋白。 菌毛蛋白前导肽的切割不依赖于已知的信号肽酶，如通过在有条件地缺乏前导肽酶生产或在抗生素球霉素存在下生长的大肠杆菌菌株中的菌毛蛋白加工概况所证明的。 此外，菌毛蛋白裂解不依赖于SecA蛋白，如叠氮化物处理的细胞中的TcpA加工所证明的。 这些结果表明，TcpJ是一类新的蛋白质参与SecA独立的蛋白水解裂解的一组非典型的前导肽在细胞外输出的代表。
Biogenesis of the Vibrio cholerae toxin-coregulated pilus (TCP) requires the activities of at least seven accessory proteins. We demonstrate that a portion of this pathway involves a novel processing step in which a hydrophilic leader peptide is proteolytically removed from TcpA by the gene product characterized in this report, TcpJ, to yield the mature, export-competent form of the pilin. Cleavage of the pilin leader peptide is independent of known signal peptidases as demonstrated by pilin-processing profiles in Escherichia coli strains conditionally defective for production of leader peptidase or grown in the presence of the antibiotic globomycin. Additionally, pilin cleavage did not rely on the SecA protein, as evidenced by TcpA processing in azide-treated cells. These results suggest that TcpJ is representative of a new class of proteins involved in SecA-independent proteolytic cleavage of a set of atypical leader peptides during extracellular export.