Extracytoplasmic proteins of Mycobacterium tuberculosis - mature secreted proteins often start with aspartic acid and proline.

Extracytoplasmic proteins of Mycobacterium tuberculosis - mature secreted proteins often start with aspartic acid and proline.
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结核分枝杆菌的胞浆外蛋白——成熟的分泌蛋白通常以天冬氨酸和脯氨酸开始。

DOI:
10.1099/00221287-146-7-1525
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发表时间:
2000
期刊:
Microbiology (Reading, England)
影响因子:
--
通讯作者:
Schoolnik,GaryK
Schoolnik,GaryK
中科院分区:
--
文献类型:
--
作者:
Wiker,HaraldG;Wilson,MikeA;Schoolnik,GaryK

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A surrogate expression system, based on fusions to thephoAbacterial reporter gene, was used to identifyMycobacterium tuberculosisgenes that encode exported proteins and the promoter regions required for their expression in the heterologous hostMycobacterium smegmatis. To assess these results in the context of the completeM. tuberculosisgenome sequence, the corresponding genes were identified and computational algorithms were employed to identify signal peptide (SP), transmembrane domain and membrane lipoprotein attachment motifs. This information was used to predict the subset ofM. tuberculosisgenes that encode exported proteins. Of the 34 genes identified by thephoAmethod, 22 were classified to encode potential soluble secreted proteins. Among these, 14 genes may encode novel secreted proteins. Six of the remaining 12 genes were predicted to encode membrane lipoproteins and an additional six to encode integral membrane proteins. Published observations of proteins proven to be secreted intoM. tuberculosisculture filtrates were reviewed to further characterize the mycobacterial SP motif. It was concluded that mycobacterial SPs are comparable in size to Gram-positive SPs, but certain features are different. In particular, arginine was the predominant N-terminally positively charged amino acid in contrast to lysine in the Gram-positives. The hydrophobic transmembrane segment of the SP was dominated by alanine, in contrast to leucine. At the C-terminal end of the SPs, the (−3, −1) rule (AXA motif) holds, with alanine as the dominant amino acid in both positions, being most dominant in the (−1) position. A high proportion of mature sequences start with aspartic acid in the (+1) position and proline in the (+2) position – the DP motif. The authors propose that the DP sequence serves as a sorting signal, following translocation and cleavage by signal peptidase I. Alternatively, the DP motif may be part of the recognition site for the signal peptidase.
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