The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis

Nilsson, Rune‐Pär; Beijer, Lena; Rutberg, Blanka

doi:10.1099/00221287-140-4-723

Cited by 46 publications

(44 citation statements)

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“…tagB, fmhA or scdA). Additionally, we observed decreased expression of glpQ in the nsaS mutant, which is part of the glycerol utilization pathway (Nilsson et al, 1994). Analysis of S. aureus cells that are deprived of their ability to utilize glycerol reveals major remodelling of the cell envelope and an accumulation of fatty acids in the cell resulting from a failure to incorporate them into the phospholipid membrane (Ray et al, 1972).…”

Section: Discussionmentioning

confidence: 99%

NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus

et al. 2011

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Staphylococcus aureus possesses 16 two-component systems (TCSs), two of which (GraRS and NsaRS) belong to the intramembrane-sensing histidine kinase (IM-HK) family, which is conserved within the firmicutes. NsaRS has recently been documented as being important for nisin resistance in S. aureus. In this study, we present a characterization of NsaRS and reveal that, as with other IM-HK TCSs, it responds to disruptions in the cell envelope. Analysis using a lacZ reporter-gene fusion demonstrated that nsaRS expression is upregulated by a variety of cell-envelope-damaging antibiotics, including phosphomycin, ampicillin, nisin, gramicidin, carbonyl cyanide m-chlorophenylhydrazone and penicillin G. Additionally, we reveal that NsaRS regulates a downstream transporter NsaAB during nisin-induced stress. NsaS mutants also display a 200-fold decreased ability to develop resistance to the cell-wall-targeting antibiotic bacitracin. Microarray analysis reveals that the transcription of 245 genes is altered in an nsaS mutant, with the vast majority being downregulated. Included within this list are genes involved in transport, drug resistance, cell envelope synthesis, transcriptional regulation, amino acid metabolism and virulence. Using inductively coupled plasma-MS we observed a decrease in intracellular divalent metal ions in an nsaS mutant when grown under low abundance conditions. Characterization of cells using electron microscopy reveals that nsaS mutants have alterations in cell envelope structure. Finally, a variety of virulence-related phenotypes are impaired in nsaS mutants, including biofilm formation, resistance to killing by human macrophages and survival in whole human blood. Thus, NsaRS is important in sensing cell damage in S. aureus and functions to reprogram gene expression to modify cell envelope architecture, facilitating adaptation and survival.

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Section: Discussionmentioning

confidence: 99%

NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus

et al. 2011

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“…G3P is then actively transported into the cytoplasm by the transmembrane inner membrane protein, G3P transporter protein, or permease (GlpT) (29), where it is utilized in lipid biosynthesis or further processed by aerobic G3P dehydrogenase (GlpD) into dihydroxyacetone phosphate and used in the glycolytic pathway. The glpT and glpQ genes of E. coli and Bacillus subtilis and the glpQ gene of H. influenzae (Hpd) have been cloned and shown to be highly conserved (23,36,59).…”

Section: Vol 179 1997mentioning

confidence: 99%

Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Shang¹,

Skare²,

Erdjument‐Bromage³

et al. 1997

J Bacteriol

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We report the purification, molecular cloning, and characterization of a 40-kDa glycerophosphodiester phosphodiesterase homolog from Borrelia hermsii. The 40-kDa protein was solubilized from whole organisms with 0.1% Triton X-100, phase partitioned into the Triton X-114 detergent phase, and purified by fastperformance liquid chromatography (FPLC). The gene encoding the 40-kDa protein was cloned from a B. hermsii chromosomal DNA lambda EXlox expression library and identified by using affinity antibodies generated against the purified native protein. The deduced amino acid sequence included a 20-amino-acid signal peptide encoding a putative leader peptidase II cleavage site, indicating that the 40-kDa protein was a lipoprotein. Based on significant homology (31 to 52% identity) of the 40-kDa protein to glycerophosphodiester phosphodiesterases of Escherichia coli (GlpQ), Bacillus subtilis (GlpQ), and Haemophilus influenzae (Hpd; protein D), we have designated this B. hermsii 40-kDa lipoprotein a glycerophosphodiester phosphodiesterase (Gpd) homolog, the first B. hermsii lipoprotein to have a putative functional assignment. A nonlipidated form of the Gpd homolog was overproduced as a fusion protein in E. coli BL21(DE3)(pLysE) and was used to immunize rabbits to generate specific antiserum. Immunoblot analysis with anti-Gpd serum recognized recombinant H. influenzae protein D, and conversely, antiserum to H. influenzae protein D recognized recombinant B. hermsii Gpd (rGpd), indicating antigenic conservation between these proteins. Antiserum to rGpd also identified native Gpd as a constituent of purified outer membrane vesicles prepared from B. hermsii. Screening of other pathogenic spirochetes with anti-rGpd serum revealed the presence of antigenically related proteins in Borrelia burgdorferi, Treponema pallidum, and Leptospira kirschneri. Further sequence analysis both upstream and downstream of the Gpd homolog showed additional homologs of glycerol metabolism, including a glycerol-3-phosphate transporter (GlpT), a glycerol-3-phosphate dehydrogenase (GlpD), and a thioredoxin reductase (TrxB).The pathogenic spirochete Borrelia hermsii is one of the etiologic agents of tick-borne relapsing fever. Infection in humans and other vertebrates is commonly characterized by recurring episodes of high fever and bacteremia with intermittent afebrile periods (55). In humans, other clinical manifestations may include pronounced muscle and joint pains, splenomegaly, hepatomegaly, jaundice, and rash, as well as respiratory, cardiovascular, and central nervous system involvement (7). The well-documented relapse phenomenon is associated with the ability of these organisms to undergo multiphasic antigenic variation during the course of disease (56). A major surfaceexposed lipoprotein designated the variable membrane protein (Vmp) has been correlated with this antigenic variation (4, 9, 11). This switching from an initial Vmp type to another prior to the establishment of a protective antibody response is thought to enable the escape of...

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“…4) is involved in the uptake and catabolism of glycerol and glycerol-3-phosphate (G3P). It contains four operons: glpP, glpFK, glpD and glpTQ (Lindgren and Rutberg, 1974;Holmberg et al, 1990;Beijer et al, 1993;Nilsson et al, 1994 an antiterminator protein, glpF encodes a glycerol uptake facilitator, glpK a glycerol kinase, glpD a G3P dehydrogenase, glpT a G3P permease and glpQ a glycerophosphodiester phosphodiesterase. The leaders of glpFK, glpD and glpTQ contain sequences which define transcription terminators.…”

Section: The Glp Regulon Of B Subtilismentioning

confidence: 99%

Antitermination of transcription of catabolic operons

Rutberg¹

1997

Molecular Microbiology

103

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SummaryAntitermination of transcription mediated by proteins interacting with mRNA sequences is described for nine operons/regulons. Eight of the systems are catabolic, while the ninth, the Klebsiella pneumoniae nas regulon, is involved in the assimilation of nitrate and nitrite. Six of the catabolic operons/regulons are found in Bacillus subtilis, one is found in Escherichia coli, and one in Pseudomonas aeruginosa. The antitermination system of five of the operons/regulons (E. coli blg, and sacPA, sacB, bgl, and lic from B. subtilis) are assigned to the bgl-sac family on the basis of extensive similarities with regard to antiterminator proteins and the sequences of the antiterminators. Other members of the bgl-sac family are the arb operon of Erwinia chrysanthemi and a presumed bgl operon of Lactococcus lactis. The antitermination systems of the other four operons/regulons (B. subtilis glp, B. subtilis hut, P. aeruginosa ami, and K. pneumoniae nas) seem to be unrelated both to the bgl-sac family and to each other. The antiterminator protein of the B. subtilis glp regulon has been found not only to cause antitermination but also to stabilize the resultant mRNA and to mediate glucose repression. If other antiterminator proteins, and antitermination factors, also prove to have additional functions, it will broaden the impact of antitermination as a means of controlling gene expression.

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The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis

Cited by 46 publications

References 3 publications

NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus

NsaRS is a cell-envelope-stress-sensing two-component system of Staphylococcus aureus

Sequence analysis and characterization of a 40-kilodalton Borrelia hermsii glycerophosphodiester phosphodiesterase homolog

Antitermination of transcription of catabolic operons

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