Effect of Accessory Proteins P19 and P20 on Cytolytic Activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli

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作者：
Robert Manasherob
Arieh Zaritsky
Eitan Ben-Dov
Deepak Saxena
Ze'ev Barak
Monica Einav
机构：
[1] Department of Life Sciences,
[2] Ben-Gurion University of the Negev,undefined
[3] P.O. Box 653,undefined
[4] Be'er-Sheva 84105,undefined
[5] Israel,undefined
[6] The Research Institute,undefined
[7] The College of Judea and Samaria,undefined
[8] Ariel 44837,undefined
[9] Israel,undefined
来源：
Current Microbiology | 2001年 / 43卷
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摘要：
The gene coding for the accessory protein P19 of Bacillus thuringiensis subsp. israelensis was expressed in Escherichia coli and its product was characterized. To investigate its putative role in δ-endotoxin crystallization as a P20-like polypeptide, each of the two encoding genes, p20 and p19, was cloned for inducible expression coordinatively with cyt1Aa. The latter is known to kill its transgenic host. P20 but not P19 stabilized Cyt1Aa and protected the host cells from its lethal effect. Neither GroEL nor GroES, expressed in trans, affected Cyt1Aa as did P20. The function of P20 is thus more specific than that of the chaperones, but that of P19 remains enigmatic. The correct sequence of p19, confirmed in all five isolates of B. thuringiensis subsp. israelensis, does not explain the slow electrophoretic mobility of its 179 amino acids product.
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页码：355 / 364
页数：9
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