Insertion of IS2 creates a novel ampC promoter in Escherichia coli

Jaurin, Bengtåke; Normark, Staffan

doi:10.1016/0092-8674(83)90067-3

Cited by 104 publications

(74 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…When the fucosepositive pseudorevertants, ECL56 (from strain ECL3) and ECL459 (from strain ECL421), were probed for the presence J. BACTERIOL. of IS5 in the HindIII1-HindIII2 region, the insertion element DNA and a section of inserted DNA (19,22,23). In the case was still there (Fig.…”

Section: Resultsmentioning

confidence: 99%

Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol

1989

View full text Add to dashboard Cite

L-1,2-Propanediol is an irretrievable end product of L-fucose fermentation by Escherichia coli. Selection for increased aerobic growth rate on propanediol results in the escalation of basal synthesis of the NAD+-linked oxidoreductase encoded by fucO, a member of thefuc regulon for the utilization of L-fucose. In general, when fucO becomes constitutively expressed, two other simultaneous changes occur: the fucA gene encoding fuculose-1-phosphate aldolase becomes constitutively expressed and the fucPIK operon encoding fucose permease, fucose isomerase, and fuculose kinase becomes noninducible. In the present study, we show that fucO and fucA form an operon which is divergently transcribed from the adjacent fucPIK operon. In propanediol-positive and fucose-negative mutants the cis-controliing region shared by the operonsfucAO and fucPIK is lengthened by 1.2 kilobases. DNA hybridization identified the insertion element to be IS5. This element, always oriented in the same direction with the left end (the BglII end) proximal to fucA, apparently causes constitutive expression offucAO and noninducibility of fucPIK. The DNA of the fucAO operon and a part of the adjacent fucP was sequenced.Following the discovery that a genetic derepression of ribitol dehydrogenase in Klebsiella pneumoniae conferred a growth ability on xylitol (27, 33), we tried to find other models of experimental evolution for assessing the importance of regulatory mutations in the acquisition of novel functions (for a review, see reference 30). During this search, we discovered that Escherichia coli can give rise to mutants that utilize L-1,2-propanediol aerobically as a sole source of carbon and energy. Serial selection on the compound resulted in the emergence of a mutant (ECL3) which grew on the novel carbon and energy source at a rate close to that on glycerol. This mutant produced constitutively an NAD+-linked oxidoreductase active on L-1,2-propanediol (46). The proximity of the locus specifying this enzyme activity and the fuc locus (at min 60) specifying the growth ability on L-fucose led us to ask whether there was a link between the metabolism of the two compounds. When the propanediol-positive mutant was tested with fucose as a carbon and energy source, growth no longer occurred (13).Previous work, together with our further studies (13), revealed the biochemical connection between the two metabolic pathways (Fig. 1). The dissimilation of fucose by wild-type E. coli requires the sequential action of fucose permease (encoded byfucP), fucose isomerase (encoded by fucf), fucose kinase (encoded by fucK), and fuculose-lphosphate aldolase (encoded by fucA). The last enzyme catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, the aldehyde is reduced to L-1,2-propanediol by an NAD+-linked oxidoreductase (encoded by fucO) and excreted into the medium. Under aerobic conditions, the aldehyde is oxidized to Llactate and then to pyruvate which enters the general metabolic pool. The inducer of the fucose syst...

show abstract

Section: Resultsmentioning

confidence: 99%

Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol

1989

View full text Add to dashboard Cite

show abstract

“…The AmpC fl-lactamase of E. coli is specifically expressed in direct proportion with growth rate [18]. The chromosomal ampC gene is controlled by a promoter which lies within the coding sequence ofthe neighboring and overlapping fumarate reductase operon (frd) [19].…”

Section: Growth Rate Control Of Ampc Syn-thesis and Murein Structurementioning

confidence: 99%

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Bishop¹,

Weiner²

1992

FEBS Letters

View full text Add to dashboard Cite

In the periplasmic space of F.sche~'ichia coil, the (L)-m-A,pm-(D)-m-A,pm pcptid¢, the lipoprotein, and the AmpC fl-lactamas¢ are controlled by growth rate. To explain this coordinate regulation, it is proposed that the AmpC protein functions as an LD-endopeptidase in addition to its known function as a fl-lactamas¢. As LD-peptides, vo-peptides and fl-lactams are structurally similar, to-peptidases may belong to the larger family of DD-peptidases and serine ~-lactamases. In contrast to K coll. many related bacteria possess an inducible AmpC protein. Several gene systems necessary for AmpC induction are known to affect various aspects of peptidoglyean metabolism, It is proposed that AmpC induction ¢o=urs indirectly via a recyclabl¢ e¢ll wall pcptid¢.

show abstract

“…ISAba2, a novel insertion sequence, and IS18 provided hybrid promoters enhancing bla OXA-58 expression. Such hybrid promoters generated upon transposition have been already observed, for instance, with IS1 and IS2 (14,23) and also with IS18. Indeed, similar to our observations, IS18 identified previously also from an A. baumannii isolate activated a silent aminoglycoside resistance gene by providing a Ϫ35 promoter sequence of an hybrid promoter (24).…”

Section: Discussionmentioning

confidence: 99%

Acinetobacter baumannii

2015

Reviews in Medical Microbiology

View full text Add to dashboard Cite

Genetic structures surrounding the carbapenem-hydrolyzing oxacillinase gene bla OXA-58 were characterized in a series of OXA-58-positive Acinetobacter baumannii strains isolated from different countries. We showed that in most of the cases, acquisitions of the bla OXA-58 -containing overall structure, including insertion sequence elements, may be likely the results of recombination events. In type strain A. baumannii MAD, the genetic structure surrounding the bla OXA-58 gene was bracketed by two 27-bp repeated sequences. The isolation of a clonally related OXA-58-negative A. baumannii isolate that possessed the same plasmid backbone as A. baumannii MAD but lacked this genetic structure indicated that the mechanism of acquisition could be reversible. Parts of the structure identified in A. baumannii MAD were conserved in other bla OXA-58 -positive isolates from various European countries. Primer extension experiments showed that bla OXA-58 expression was related to promoter sequences brought by different insertion sequence elements, such as an ISAba3-like element, ISAba1, ISAba2, and IS18. This work identified novel structures at the origin of acquisition and expression of a carbapenem-hydrolyzing ␤-lactamase identified in non-clonally related A. baumannii isolates.

show abstract

Insertion of IS2 creates a novel ampC promoter in Escherichia coli

Cited by 104 publications

References 33 publications

Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol

Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Acinetobacter baumannii

Contact Info

Product

Resources

About