Effect of accessory proteins P19 and P20 on cytolytic activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli

Robert Manasherob; Arieh Zaritsky; Eitan Ben-Dov; Deepak Saxena; Ze'ev Barak; Monica Einav

doi:10.1007/s002840010316

Effect of accessory proteins P19 and P20 on cytolytic activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli

Robert Manasherob, Arieh Zaritsky, Eitan Ben-Dov, Deepak Saxena, Ze'ev Barak, Monica Einav

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	355-364
Number of pages	10
Journal	Current Microbiology
Volume	43
Issue number	5
DOIs	https://doi.org/10.1007/s002840010316
State	Published - 2001

ASJC Scopus subject areas

Microbiology
Applied Microbiology and Biotechnology

Access to Document

10.1007/s002840010316

Cite this

@article{ff74348cd2c14a89b85f93013503d756,

title = "Effect of accessory proteins P19 and P20 on cytolytic activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli",

abstract = "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.",

author = "Robert Manasherob and Arieh Zaritsky and Eitan Ben-Dov and Deepak Saxena and Ze'ev Barak and Monica Einav",

year = "2001",

doi = "10.1007/s002840010316",

language = "English (US)",

volume = "43",

pages = "355--364",

journal = "Current Microbiology",

issn = "0343-8651",

publisher = "Springer New York",

number = "5",

}

TY - JOUR

T1 - Effect of accessory proteins P19 and P20 on cytolytic activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli

AU - Manasherob, Robert

AU - Zaritsky, Arieh

AU - Ben-Dov, Eitan

AU - Saxena, Deepak

AU - Barak, Ze'ev

AU - Einav, Monica

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0034763147&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034763147&partnerID=8YFLogxK

U2 - 10.1007/s002840010316

DO - 10.1007/s002840010316

M3 - Article

C2 - 11688801

AN - SCOPUS:0034763147

SN - 0343-8651

VL - 43

SP - 355

EP - 364

JO - Current Microbiology

JF - Current Microbiology

IS - 5

ER -

Effect of accessory proteins P19 and P20 on cytolytic activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis in Escherichia coli

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this