Organization of heat shock dnaK and groE operons of the nosocomial pathogen Enterococcus faecium

Laport, Marinella Silva; Santos, Leonardo Lima dos; Lemos, José A.; Bastos, Maria do Carmo F.; Burne, Robert A.; Giambiagi-deMarval, Márcia

doi:10.1016/j.resmic.2005.06.010

Cited by 12 publications

(8 citation statements)

References 19 publications

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“…These HSPs were translated from mRNA dnak and groES genes (Cardoso et al, 2010). In agreement with Laport et al (2006), who noted that not only changes in temperature trigger the HSPs expression in bacteria. Caillet et al (2008) noticed a significant induction of Dnak and GroeS proteins in E. coli in response to γ-radiation at dose 0.4-1.3kGy.…”

Section: Introductionsupporting

confidence: 79%

Expression of dnak, groES and cps genes in irradiated Klebsiella pneumoniae strains isolated from UTI Egyptian patients

Nada

Hagag²,

El-Tablawy

2019

Egypt. J. Rad.Sci.

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Section: Introductionsupporting

confidence: 79%

Expression of dnak, groES and cps genes in irradiated Klebsiella pneumoniae strains isolated from UTI Egyptian patients

Nada

Hagag²,

El-Tablawy

2019

Egypt. J. Rad.Sci.

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“…The genetic organization of the dnaK operon in L. gasseri ATCC 33323 is typical for other firmicutes (data not shown) where the first gene in the operon encodes HrcA, the autorepressor of the operon. Multiple heat-induced transcripts detected with hrcA-specific probe may result from post-transcriptional processing of the hrcA-operon mRNA observed in several other bacteria [44][45][46][47].…”

Section: Discussionmentioning

confidence: 94%

ClpL is essential for induction of thermotolerance and is potentially part of the HrcA regulon in Lactobacillus gasseri

et al. 2008

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Stress-inducible proteins are likely to contribute to the survival and activity of probiotic bacteria during industrial processes and in the gastrointestinal tract. The recently published genome sequence of probiotic Lactobacillus gasseri ATCC 33323 suggests the presence of ClpC, ClpE, ClpL, and ClpX from the Clp ATPase family of stress proteins. The heat-shock response of L. gasseri was studied using 2-D DIGE. A total of 20 protein spots showing significant (p<0.05) increase in abundance after 30 min heat-shock were identified, including DnaK, GroEL, ClpC, ClpE, and ClpL. To study the physiological role of ClpL, one of the most highly induced proteins during heat-shock, its corresponding gene was inactivated. The DeltaclpL mutant strain had growth characteristics that were indistinguishable from wild-type under several stress conditions. However, in the absence of functional ClpL, L. gasseri exhibited drastically reduced survival at a lethal temperature and was unable to induce thermotolerance. Genome sequences indicate that the expression of clp genes in several Lactobacillus species is regulated by HrcA, instead of CtsR, the conserved clp gene regulator of low G+C Gram-positive bacteria. Electrophoretic mobility shift assays using L. gasseri HrcA protein and clpL upstream fragments revealed, for the first time, a direct interaction between HrcA and the promoter of a clp gene from a Lactobacillus.

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“…Accordingly, many molecular chaperones are also referred to as heat-shock proteins (HSPs) including the GroEL and GroES proteins. However, it should be mentioned that also other stress conditions including salt or ethanol stress are known to influence groEL expression in some bacteria (Laport et al, 2006;Camarena et al, 2010). A specific sigma factor, RpoH, is recognizing a characteristic consensus promoter motif and is triggering the heat-shock response in many bacteria (Guisbert et al, 2008).…”

Section: Groel As An Essential Symbiosis Factor In Bacteria-insect Inmentioning

confidence: 99%

Versatile roles of the chaperonin GroEL in microorganism-insect interactions

Kupper

Gupta

Feldhaar³

et al. 2014

FEMS Microbiol Lett

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The chaperonin 60 (Cpn60) is present in all three kingdoms of life and is one of the most conserved proteins in living organisms. The Escherichia coli Cpn60 (GroEL) is the best studied representative of the huge Cpn60 family. It is an essential protein because in conjunction with the chaperonin 10 (Cpn10 or GroES) it forms a protein-folding machine required for correct folding of many proteins and for recycling of misfolded proteins. As many other chaperones, GroEL and GroES are also known as heat-shock proteins (HSPs), since heat stress leads to a strong induction of their expression, a measure to counteract the increase in misfolded proteins as a result of a high nonphysiological temperature. A large amount of literature is available which is dedicated to the elucidation of how protein folding is assisted by this molecular chaperone. However, apart from this primary task, additional so-called 'moonlighting' functions of GroEL proteins unrelated to their folding activity have emerged in the past years. In fact, it becomes apparent that GroEL proteins have diverse functions in particular in mutualistic and pathogenic microorganism-host interactions. In this brief review, we describe some of these recent findings focusing on the importance of GroEL for microorganism-insect interactions.

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Organization of heat shock dnaK and groE operons of the nosocomial pathogen Enterococcus faecium

Cited by 12 publications

References 19 publications

Expression of dnak, groES and cps genes in irradiated Klebsiella pneumoniae strains isolated from UTI Egyptian patients

Expression of dnak, groES and cps genes in irradiated Klebsiella pneumoniae strains isolated from UTI Egyptian patients

ClpL is essential for induction of thermotolerance and is potentially part of the HrcA regulon in Lactobacillus gasseri

Versatile roles of the chaperonin GroEL in microorganism-insect interactions

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