The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock

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The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. / Kuczynska-Wisnik, D; Kedzierska, S; Matuszewska, E; Lund, Peter; Taylor, A; Lipinska, B; Laskowska, E.

In: Microbiology, Vol. 148, 01.06.2002, p. 1757-1765.

Research output: Contribution to journalArticle

Harvard

Kuczynska-Wisnik, D, Kedzierska, S, Matuszewska, E, Lund, P, Taylor, A, Lipinska, B & Laskowska, E 2002, 'The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock', Microbiology, vol. 148, pp. 1757-1765.

APA

Kuczynska-Wisnik, D., Kedzierska, S., Matuszewska, E., Lund, P., Taylor, A., Lipinska, B., & Laskowska, E. (2002). The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology, 148, 1757-1765.

Vancouver

Author

Kuczynska-Wisnik, D ; Kedzierska, S ; Matuszewska, E ; Lund, Peter ; Taylor, A ; Lipinska, B ; Laskowska, E. / The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. In: Microbiology. 2002 ; Vol. 148. pp. 1757-1765.

Bibtex

@article{d199d7af54f24bd8ae089a1fb62b7ffb,
title = "The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock",
abstract = "The roles of the Escherichia coli lbpA and lbpB chaperones in protection of heat-denatured proteins against irreversible aggregation in vivo were investigated. Overproduction of lbpA and lbpB resulted in stabilization of the denatured and reversibly aggregated proteins (the S fraction), which could be isolated from E. coli cells by sucrose gradient centrifugation. This finding is in agreement with the present model of the small heat-shock proteins' function, based mainly on in vitro studies. Deletion of the ibpAB operon resulted in almost twofold increase in protein aggregation and in inactivation of an enzyme (fructose-1,6-biphosphate aldolase) in cells incubated at 50 degreesC for 4 h, decreased efficiency of the removal of protein aggregates formed during prolonged incubation at 50 degreesC and affected cell viability at this temperature. IbpA/B proteins were not needed for removal of protein aggregates or for the enzyme protection/renaturation in cells heat shocked at 50 degreesC for 15 min. These results show that the IbpA/B proteins are required upon an extreme, long-term heat shock. Overproduction of lbpA but not lbpB caused an increase of the level of beta-lactamase precursor, which was localized in the S fraction, together with the lbpA protein, which suggests that the unfolded precursor binds to lbpA but not to lbpB. Although in the wild-type cells both E. coli small heat-shock proteins are known to localize in the S fraction, only 2% of total lbpB co-localized with the aggregated proteins in the absence of lbpA, while in the absence of lbpB, the majority of lbpA was present in the aggregates fraction.",
keywords = "protein aggregation, beta-lactamase precursor, DnaK",
author = "D Kuczynska-Wisnik and S Kedzierska and E Matuszewska and Peter Lund and A Taylor and B Lipinska and E Laskowska",
year = "2002",
month = jun,
day = "1",
language = "English",
volume = "148",
pages = "1757--1765",
journal = "Microbiology",
issn = "1350-0872",
publisher = "Society for General Microbiology",

}

RIS

TY - JOUR

T1 - The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock

AU - Kuczynska-Wisnik, D

AU - Kedzierska, S

AU - Matuszewska, E

AU - Lund, Peter

AU - Taylor, A

AU - Lipinska, B

AU - Laskowska, E

PY - 2002/6/1

Y1 - 2002/6/1

N2 - The roles of the Escherichia coli lbpA and lbpB chaperones in protection of heat-denatured proteins against irreversible aggregation in vivo were investigated. Overproduction of lbpA and lbpB resulted in stabilization of the denatured and reversibly aggregated proteins (the S fraction), which could be isolated from E. coli cells by sucrose gradient centrifugation. This finding is in agreement with the present model of the small heat-shock proteins' function, based mainly on in vitro studies. Deletion of the ibpAB operon resulted in almost twofold increase in protein aggregation and in inactivation of an enzyme (fructose-1,6-biphosphate aldolase) in cells incubated at 50 degreesC for 4 h, decreased efficiency of the removal of protein aggregates formed during prolonged incubation at 50 degreesC and affected cell viability at this temperature. IbpA/B proteins were not needed for removal of protein aggregates or for the enzyme protection/renaturation in cells heat shocked at 50 degreesC for 15 min. These results show that the IbpA/B proteins are required upon an extreme, long-term heat shock. Overproduction of lbpA but not lbpB caused an increase of the level of beta-lactamase precursor, which was localized in the S fraction, together with the lbpA protein, which suggests that the unfolded precursor binds to lbpA but not to lbpB. Although in the wild-type cells both E. coli small heat-shock proteins are known to localize in the S fraction, only 2% of total lbpB co-localized with the aggregated proteins in the absence of lbpA, while in the absence of lbpB, the majority of lbpA was present in the aggregates fraction.

AB - The roles of the Escherichia coli lbpA and lbpB chaperones in protection of heat-denatured proteins against irreversible aggregation in vivo were investigated. Overproduction of lbpA and lbpB resulted in stabilization of the denatured and reversibly aggregated proteins (the S fraction), which could be isolated from E. coli cells by sucrose gradient centrifugation. This finding is in agreement with the present model of the small heat-shock proteins' function, based mainly on in vitro studies. Deletion of the ibpAB operon resulted in almost twofold increase in protein aggregation and in inactivation of an enzyme (fructose-1,6-biphosphate aldolase) in cells incubated at 50 degreesC for 4 h, decreased efficiency of the removal of protein aggregates formed during prolonged incubation at 50 degreesC and affected cell viability at this temperature. IbpA/B proteins were not needed for removal of protein aggregates or for the enzyme protection/renaturation in cells heat shocked at 50 degreesC for 15 min. These results show that the IbpA/B proteins are required upon an extreme, long-term heat shock. Overproduction of lbpA but not lbpB caused an increase of the level of beta-lactamase precursor, which was localized in the S fraction, together with the lbpA protein, which suggests that the unfolded precursor binds to lbpA but not to lbpB. Although in the wild-type cells both E. coli small heat-shock proteins are known to localize in the S fraction, only 2% of total lbpB co-localized with the aggregated proteins in the absence of lbpA, while in the absence of lbpB, the majority of lbpA was present in the aggregates fraction.

KW - protein aggregation

KW - beta-lactamase precursor

KW - DnaK

M3 - Article

C2 - 12055295

VL - 148

SP - 1757

EP - 1765

JO - Microbiology

JF - Microbiology

SN - 1350-0872

ER -