Protein synthesis patterns inAcinetobacter calcoaceticusinduced by phenol and catechol show specificities of responses to chemostress

Abstract

The proteins induced in Acinetobacter calcoaceticus by the potentially toxic growth substrates phenol and catechol were analyzed by 2D-electrophoresis of cell extracts and compared with those induced by heat shock and oxidative stress. Although both aromatic compounds are quite similar, the only difference being that catechol has an additional hydroxyl group, the responses obtained differed considerably. Phenol has greater lipophilicity and mainly induced heat shock proteins, whereas catechol, which causes the production of reactive oxygen species, predominantly induced oxidative stress proteins. Furthermore, some special proteins were induced by phenol or catechol, which might be useful as biomarkers for chemostress, and could be involved in the catalytic degradation of potentially toxic compounds.

Assimilatory detoxification of herbicides by Delftia acidovorans MC1: induction of two chlorocatechol 1,2-dioxygenases as a response to chemostress The SWISS-PROT accession numbers for the sequences reported in this paper are P83115, P83116 and P83117.

“…This was surprising and interesting insofar as a high degree of lipophilicity has proven to be a common property of chemicals that induce heat-shock proteins, e.g. primary alcohols in A. calcoaceticus 69-V (Benndorf et al, 1999(Benndorf et al, , 2001. A further important property of potential stress chemicals, which may account for the induction of other groups of stress proteins, is their reactivity.…”

“…A further important property of potential stress chemicals, which may account for the induction of other groups of stress proteins, is their reactivity. For example, A. calcoaceticus 69-V synthesizes oxidative stress proteins in response to catechol (Benndorf et al, 2001), which detoxifies reactive oxygen species generated by redox cycling (Schweigert et al, 2001). It is also noteworthy that the reactive compound 3,5-DCC induced no change in the level of alkylhydroperoxide reductase subunit C, which is strongly induced by hydrogen peroxide.…”

“…Previous studies have shown heat-shock proteins to be induced by a variety of mainly hydrophobic compounds and these chaperones may defend cells against the toxic effects of such compounds (Benndorf et al, 1999). An example of an D. Benndorf and W. Babel active protection mechanism is the induction of the oxidative stress response in Acinetobacter calcoaceticus, which increases the organism's resistance to catechol by detoxifying reactive oxygen species released by redox cycling (Benndorf et al, 2001). The induction of further groups of proteins associated with responses to starvation (Blom et al, 1992), osmotic shock and pH shock (Vasseur et al, 1999) has also been observed.…”

A proteomic analysis of Psychrobacter articus 273‐4 adaptation to low temperature and salinity using a 2‐D liquid mapping approach

“…NaCl may stimulate cells to generate alkyl hydroperoxide at 227C. These reductases were induced by the salt at 227C as they were induced by other oxidative stress [55]. Similar to the response to temperature in the cells cultured in the 1/2 TSB, HSP10, HSP60, the coldshock protein, EF-Tu, DNA-directed RNA polymerase, peptidyl-prolyl cis-trans isomerase, cyclophilin-type, ribosomal protein S3, ribosomal protein L2, two conserved hypothetical proteins encoded from genes 2392 and 935, and a number of metabolism-related proteins were up-regulated in response to salinity at 227C while some other ribosomal proteins were down-regulated.…”

The effects of divalent copper on performance, extracellular polymeric substances and microbial community of an anoxic–aerobic sequencing batch reactor

“…The effects of Cu(II) on the PN and PS contents in the LB-EPS and TB-EPS are illustrated in Fig. 7 Benndorf et al 26 reported that the elevated production of PN was the induction of heat shock-like proteins as a defense mechanism against high heavy metal ion concentrations. As the EPS matrix could form a protective shield for the cells against the toxicity of Cu(II), the PN and PS contents in the LB-EPS and TB-EPS gradually increased with the increase of Cu(II) concentration.…”