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J Bacteriol. 1997 Sep;179(18):5959-62. doi: 10.1128/jb.179.18.5959-5962.1997.
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本文引用的文献

1
THE CONDENSATION REACTION OF FATTY ACID SYNTHESIS.III. IDENTIFICATION OF THE PROTEIN-BOUND PRODUCT OF THE REACTION AND ITS CONVERSION TO LONG CHAIN FATTY ACIDS.脂肪酸合成中的缩合反应。III. 反应中蛋白质结合产物的鉴定及其向长链脂肪酸的转化
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Structure-function studies of the adenylate cyclase toxin of Bordetella pertussis and the leukotoxin of Pasteurella haemolytica by heterologous C protein activation and construction of hybrid proteins.通过异源C蛋白激活和杂交蛋白构建对百日咳博德特氏菌腺苷酸环化酶毒素和溶血巴斯德氏菌白细胞毒素进行结构-功能研究。
J Bacteriol. 1997 Feb;179(3):871-9. doi: 10.1128/jb.179.3.871-879.1997.
3
Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.大肠杆菌溶血素（HlyA）的体内激活分析。
J Bacteriol. 1996 Sep;178(18):5422-30. doi: 10.1128/jb.178.18.5422-5430.1996.
4
Independent interaction of the acyltransferase HlyC with two maturation domains of the Escherichia coli toxin HlyA.酰基转移酶HlyC与大肠杆菌毒素HlyA的两个成熟结构域的独立相互作用。
Mol Microbiol. 1996 May;20(4):813-22. doi: 10.1111/j.1365-2958.1996.tb02519.x.
5
Escherichia coli hemolysin mutants with altered target cell specificity.具有改变的靶细胞特异性的大肠杆菌溶血素突变体。
Infect Immun. 1996 Aug;64(8):3081-7. doi: 10.1128/iai.64.8.3081-3087.1996.
6
Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7.肠出血性大肠杆菌O157:H7中RTX毒素的特性分析。
Infect Immun. 1996 Jan;64(1):167-75. doi: 10.1128/iai.64.1.167-175.1996.
7
Molecular characterization of a leukotoxin gene from a Pasteurella haemolytica-like organism, encoding a new member of the RTX toxin family.来自类溶血巴斯德氏菌的白细胞毒素基因的分子特征分析，该基因编码RTX毒素家族的一个新成员。
Infect Immun. 1993 May;61(5):2089-95. doi: 10.1128/iai.61.5.2089-2095.1993.
8
Loss of activity in the secreted form of Escherichia coli haemolysin caused by an rfaP lesion in core lipopolysaccharide assembly.核心脂多糖组装过程中rfaP损伤导致大肠杆菌溶血素分泌形式的活性丧失。
Mol Microbiol. 1993 Nov;10(4):781-7. doi: 10.1111/j.1365-2958.1993.tb00948.x.
9
Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin.大肠杆菌溶血素毒性活性所需的两个内部赖氨酸残基的脂肪酰化作用。
Science. 1994 Dec 23;266(5193):1992-6. doi: 10.1126/science.7801126.
10
Transport of hemolysin by Escherichia coli.大肠杆菌对溶血素的转运
J Cell Biochem. 1983;22(2):87-97. doi: 10.1002/jcb.240220203.

由于hlyC 3'区域的突变导致大肠杆菌溶血素（HlyA）激活不完全。

Incomplete activation of Escherichia coli hemolysin (HlyA) due to mutations in the 3' region of hlyC.

作者信息

Guzmán-Verri C, García F, Arvidson S

机构信息

Microbiology and Tumorbiology Centre (MTC), Karolinska Institute, Stockholm, Sweden.

出版信息

J Bacteriol. 1997 Sep;179(18):5959-62. doi: 10.1128/jb.179.18.5959-5962.1997.

DOI:10.1128/jb.179.18.5959-5962.1997
PMID:9294460
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC179492/
Abstract

Mutational analysis of the carboxy-terminal region of Escherichia coli HlyC was performed by site-directed mutagenesis. Replacement of residue Val-127 or Lys-129 reduced the activity of HlyC to about 30 or 60%, respectively, of that of the wild type, while replacement of Gly-128 reduced the activity to less than 1% of the wild-type level. Complete inactivation of HlyC was caused by a double mutation, replacement of Gly-128 with valine and of Lys-129 with isoleucine. Analysis of culture supernatants from mutants with reduced hemolytic activity by two-dimensional gel electrophoresis revealed the production and simultaneous secretion of nonacylated, monoacylated, and fully acylated HlyA forms, demonstrating impairment of the acylation reaction, possibly due to a decreased affinity of HlyC for the individual HlyA acylation sites.

摘要

通过定点诱变对大肠杆菌HlyC的羧基末端区域进行了突变分析。残基Val-127或Lys-129的替换分别将HlyC的活性降低至野生型的约30%或60%，而Gly-128的替换则将活性降低至野生型水平的不到1%。HlyC的完全失活是由双重突变引起的，即Gly-128被缬氨酸替换，Lys-129被异亮氨酸替换。通过二维凝胶电泳对溶血活性降低的突变体的培养上清液进行分析，结果显示了非酰化、单酰化和完全酰化的HlyA形式的产生及同时分泌，这表明酰化反应受到损害，可能是由于HlyC对各个HlyA酰化位点的亲和力降低所致。