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Tn10 四环素抗性膜蛋白的顺反子内互补作用

Intracistronic complementation of the tetracycline resistance membrane protein of Tn10.

作者信息

Curiale M S, McMurry L M, Levy S B

出版信息

J Bacteriol. 1984 Jan;157(1):211-7. doi: 10.1128/jb.157.1.211-217.1984.

DOI:10.1128/jb.157.1.211-217.1984
PMID:6317652
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC215154/
Abstract

The structural gene region for tetracycline resistance on Tn10 consists of two complementation groups, tetA and tetB (M. S. Curiale and S. B. Levy, J. Bacteriol. 151:209-215, 1982). Using a series of deletion mutants, we have determined that the tetA region is 450 to 600 base pairs long and that the tetB region, which is adjacent to tetA, is 600 to 750 base pairs long. Point mutations in either tetA or tetB affected the amount and size of the inducible inner-membrane Tet protein synthesized in Escherichia coli maxicells. Moreover, deletions in these regions led to the synthesis of an appropriately smaller Tet protein. A single tetracycline-inducible RNA of about 1,200 bases was detected that was homologous with the tetracycline resistance structural gene region. These results indicate that the tetA and tetB complementation regions represent two parts of a single gene encoding two domains of the tetracycline resistance protein Tet.

摘要

Tn10上四环素抗性的结构基因区域由两个互补群tetA和tetB组成(M. S. 库里亚莱和S. B. 利维,《细菌学杂志》151:209 - 215,1982年)。利用一系列缺失突变体,我们确定tetA区域长450至600个碱基对,与tetA相邻的tetB区域长600至750个碱基对。tetA或tetB中的点突变影响了在大肠杆菌大细胞中合成的可诱导内膜Tet蛋白的量和大小。此外,这些区域的缺失导致合成了相应更小的Tet蛋白。检测到一条约1200个碱基的单一四环素诱导型RNA,它与四环素抗性结构基因区域同源。这些结果表明,tetA和tetB互补区域代表一个单一基因的两个部分,该基因编码四环素抗性蛋白Tet的两个结构域。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2800/215154/563095dff0e1/jbacter00236-0233-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2800/215154/db9f4d846843/jbacter00236-0232-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2800/215154/563095dff0e1/jbacter00236-0233-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2800/215154/db9f4d846843/jbacter00236-0232-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2800/215154/563095dff0e1/jbacter00236-0233-a.jpg

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本文引用的文献

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Evidence that TET protein functions as a multimer in the inner membrane of Escherichia coli.有证据表明TET蛋白在大肠杆菌内膜中作为多聚体发挥作用。
J Bacteriol. 1988 Apr;170(4):1715-20. doi: 10.1128/jb.170.4.1715-1720.1988.
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