Cloning and Comparison of Third β-Glucoside Utilization (bglEFIA) Operon with Two Operons ofPectobacterium carotovorumsubsp.carotovorumLY34

Hong, Su Young; An, Chang Long; Cho, Kye Man; Lee, Sun Mi; Kim, Yong Hee; Kim, Min Keun; Cho, Soo‐Jeong; Lim, Yong Pyo; Kim, Hoon; Yun, Han Dae

doi:10.1271/bbb.70.798

Cited by 8 publications

(2 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…bglF and bglF2 are redundant for utilization of ␤-glucoside in C. glutamicum R (41). Redundant ␤-glucoside PTSs are present in other bacteria such as Streptococcus mutans and Pectobacterium carotovorum (3,15). Similar to what was shown in C. glutamicum in this study, different sensitivities of the multiple ␤-glucoside PTS genes to glucose have been reported in S. mutans although the mechanism underlying the differences in the glucose repression remains elusive.…”

Section: Discussionsupporting

confidence: 84%

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

et al. 2011

View full text Add to dashboard Cite

Corynebacterium glutamicum R has two ␤-glucoside phosphoenolpyruvate, carbohydrate phosphotransferase systems (PTS) encoded by bglF and bglF2 located in the respective clusters, bglF-bglA-bglG and bglF2-bglA2-bglG2. Previously, we reported that whereas ␤-glucoside-dependent induction of bglF is strongly repressed by glucose, glucose repression of bglF2 is very weak. Here, we reveal the mechanism behind the different effects of glucose on the two bgl genes. Deletion of the ribonucleic antiterminator sequence and transcriptional terminator located upstream of the translation initiation codon of bglF markedly relieved the glucose repression of a bglF-lacZ fusion, indicating that glucose affects the antitermination mechanism that is responsible for the ␤-glucoside-dependent induction of the bglF cluster. The glucose repression of bglF mRNA was also relieved by introducing a multicopy plasmid carrying the bglG gene encoding an antiterminator of the bglF cluster. Moreover, replacement of the GUG translation initiation codon of bglG with AUG was effective in relieving the glucose repression of bglF and bglG. Inversely, expression of bglF2 and bglG2 was subject to strict glucose repression in a mutant strain in which the AUG translation initiation codon of bglG2 encoding antiterminator of the bglF2 cluster was replaced with GUG. These results suggest that the translation initiation efficiency of the antiterminator proteins, at least in part, determines whether the target genes are subject to glucose repression. We also found that bglF expression was induced by glucose in the BglG-overexpressing strains, which may be explained by the ability of BglF to transport glucose.In many bacterial cells, ␤-glucosides are taken up via the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), which is consequently important for the acquisition of various carbohydrates (22, 34). The PTS consists of two common cytoplasmic proteins, enzyme I (EI) and HPr, and an array of carbohydrate-specific enzyme II (EII) permeases. The phosphoryl group from phosphoenolpyruvate is sequentially transferred to EI, HPr, EII, and finally to the carbohydrate as it is translocated across the membrane.An antitermination mechanism has a pivotal role in regulation of ␤-glucoside PTS genes in many bacteria. The regulation has been well studied in Escherichia coli and Bacillus subtilis. In the antitermination regulatory mechanism, transcription stops at a terminator sequence present in the 5Ј untranslated region (UTR) of the target mRNA. In the presence of substrate sugar, a transcriptional antiterminator protein of the BglG/ SacY family binds to the ribonucleic antiterminator (RAT) sequence partially overlapping the transcriptional terminator and thereby results in transcription elongation to the end of the target gene (1,5,38).An antiterminator such as E. coli BglG or B. subtilis LicT is inactivated by phosphorylation at the PTS regulation domain 1 (PRD-1) by a ␤-glucoside EII. Concomitant with PTS-dependent uptake and phosphorylation of the subs...

show abstract

Section: Discussionsupporting

confidence: 84%

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

et al. 2011

View full text Add to dashboard Cite

show abstract

“…The presence of redundant b-glucoside PTSs is found in other bacteria, such as E. coli, Streptococcus mutans and Pectobacterium carotovorum (Parker & Hall, 1988;Cote et al, 2000;Hong et al, 2006). However, there are few studies on how the expression of these b-glucoside PTSs is coordinated.…”

Section: Discussionmentioning

confidence: 99%

Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R

et al. 2009

View full text Add to dashboard Cite

The phosphoenolpyruvate : carbohydrate phosphotransferase system (PTS) catalyses carbohydrate transport by coupling it to phosphorylation. Previously, we reported a Corynebacterium glutamicum R b-glucoside PTS encoded by bglF. Here we report that C. glutamicum R contains an additional b-glucoside PTS gene, bglF2, organized in a cluster with a putative phospho-b-glucosidase gene, bglA2, and a putative antiterminator, bglG2. While single gene disruption strains of either bglF or bglF2 were able to utilize salicin or arbutin as sole carbon sources, a double disruption strain exhibited defects in utilization of both carbon sources. Expression of both bglF and bglF2 was induced in the presence of either salicin or arbutin, although disruption of bglG2 affected only bglF2 expression. Moreover, in the presence of either salicin or arbutin, glucose completely repressed the expression of bglF but only slightly repressed that of bglF2. We conclude that BglF and BglF2 have a redundant role in b-glucoside transport even though the catabolite repression control of their encoding genes is different. We also show that expression of both bglF and bglF2 requires the general PTS.

show abstract

Diverse pathways for salicin utilization in Shigella sonnei and Escherichia coli carrying an impaired bgl operon

2010

View full text Add to dashboard Cite

Utilization of the aryl-β-glucosides salicin or arbutin in most wild-type strains of E. coli is achieved by a single-step mutational activation of the bgl operon. Shigella sonnei, a branch of the diverse E. coli strain tree, requires two sequential mutational steps for achieving salicin utilization as the bglB gene, encoding the phospho-β-glucosidase B, harbors an inactivating insertion. We show that in a natural isolate of S. sonnei, transcriptional activation of the gene SSO1595, encoding a phospho-β-glucosidase, enables salicin utilization with the permease function being provided by the activated bgl operon. SSO1595 is absent in most commensal strains of E. coli, but is present in extra-intestinal pathogens as bgcA, a component of the bgc operon that enables β-glucoside utilization at low temperature. Salicin utilization in an E. coli bglB laboratory strain also requires a two-step activation process leading to expression of BglF, the PTS-associated permease encoded by the bgl operon and AscB, the phospho-β-glucosidase B encoded by the silent asc operon. BglF function is needed since AscF is unable to transport β-glucosides as it lacks the IIA domain involved in phopho-relay. Activation of the asc operon in the Sal(+) mutant is by a promoter-up mutation and the activated operon is subject to induction. The pathway to achieve salicin utilization is therefore diverse in these two evolutionarily related organisms; however, both show cooperation between two silent genetic systems to achieve a new metabolic capability under selection.

show abstract

Cloning and Comparison of Third β-Glucoside Utilization (bglEFIA) Operon with Two Operons ofPectobacterium carotovorumsubsp.carotovorumLY34

Cited by 8 publications

References 38 publications

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

Translation Efficiency of Antiterminator Proteins Is a Determinant for the Difference in Glucose Repression of Two β-Glucoside Phosphotransferase System Gene Clusters inCorynebacterium glutamicumR

Identification of a second β-glucoside phosphoenolpyruvate : carbohydrate phosphotransferase system in Corynebacterium glutamicum R

Diverse pathways for salicin utilization in Shigella sonnei and Escherichia coli carrying an impaired bgl operon

Contact Info

Product

Resources

About