Novel roles for GlcNAc in cell signaling

Naseem, Saadia; Parrino, Salvatore M.; Buenten, Dane M.; Konopka, James B.

doi:10.4161/cib.19034

Cited by 44 publications

(44 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, soils are generally carbon-rich and nitrogen-poor environments (Hodgson, 2000); GlcNAc-containing polymers are a rich source of both these essential nutrients. morphogenesis in Candida albicans (Gilmore et al, 2013;Naseem et al, 2011); (ii) siderophore biosynthesis, antibiotic production and sporulation in streptomycetes (Colson et al, 2008;Craig et al, 2012;Nazari et al, 2013;Rigali et al, 2006Rigali et al, , 2008Świątek et al, 2012a, b); (iii) altering the expression of virulence factors in pathogenic Escherichia coli (Barnhart et al, 2006;Sohanpal et al, 2004), amongst others (Konopka, 2012;Naseem et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Control of chitin and N-acetylglucosamine utilization in Saccharopolyspora erythraea

Liao

Rigali²,

Licona-Cassani

et al. 2014

Microbiology

View full text Add to dashboard Cite

Chitin degradation and subsequent N-acetylglucosamine (GlcNAc) catabolism is thought to be a common trait of a large majority of actinomycetes. Utilization of aminosugars had been poorly investigated outside the model strain Streptomyces coelicolor A3(2), and we examined here the genetic setting of the erythromycin producer Saccharopolyspora erythraea for GlcNAc and chitin utilization, as well as the transcriptional control thereof. Sacch. erythraea efficiently utilize GlcNAc most likely via the phosphotransferase system (PTSGlcNAc); however, this strain is not able to grow when chitin or N,N′-diacetylchitobiose [(GlcNAc)2] is the sole nutrient source, despite a predicted extensive chitinolytic system (chi genes). The inability of Sacch. erythraea to utilize chitin and (GlcNAc)2 is probably because of the loss of genes encoding the DasABC transporter for (GlcNAc)2 import, and genes for intracellular degradation of (GlcNAc)2 by β-N-acetylglucosaminidases. Transcription analyses revealed that in Sacch. erythraea all putative chi and GlcNAc utilization genes are repressed by DasR, whereas in Strep. coelicolor DasR displayed either activating or repressing functions whether it targets genes involved in the polymer degradation or genes for GlcNAc dimer and monomer utilization, respectively. A transcriptomic analysis further showed that GlcNAc not only activates the transcription of GlcNAc catabolism genes but also activates chi gene expression, as opposed to the previously reported GlcNAc-mediated catabolite repression in Strep. coelicolor. Finally, synteny exploration revealed an identical genetic background for chitin utilization in other rare actinomycetes, which suggests that screening procedures that used only the chitin-based protocol for selective isolation of antibiotic-producing actinomycetes could have missed the isolation of many industrially promising strains.

show abstract

Section: Introductionmentioning

confidence: 99%

Control of chitin and N-acetylglucosamine utilization in Saccharopolyspora erythraea

Liao

Rigali²,

Licona-Cassani

et al. 2014

Microbiology

View full text Add to dashboard Cite

show abstract

“…GlcNAc does not have to be catabolized to induce hyphal growth, because a strain lacking the genes needed for GlcNAc metabolism (hxk1D nag1D dac1D) can be induced to form hyphae (Naseem et al 2011. This led to the proposal that cells sensitively distinguish exogenous GlcNAc taken up from the environment vs. GlcNAc synthesized inside the cell, because exogenous GlcNAc is not phosphorylated whereas cells only synthesize phosphorylated forms of this sugar (e.g., GlcNAc-6-PO4) (Naseem et al 2012). Previous studies suggested that the cAMP pathway might be involved in GlcNAc signaling, since a cyr1D mutant that lacks adenylyl cyclase is not induced by GlcNAc to form hyphae.…”

mentioning

confidence: 99%

Regulation of Hyphal Growth and N-Acetylglucosamine Catabolism by Two Transcription Factors in Candida albicans

Naseem

Min

Spitzer³

et al. 2017

Genetics

Self Cite

View full text Add to dashboard Cite

The amino sugar N-acetylglucosamine (GlcNAc) is increasingly recognized as an important signaling molecule in addition to its well-known structural roles at the cell surface. In the human fungal pathogen Candida albicans, GlcNAc stimulates several responses including the induction of the genes needed for its catabolism and a switch from budding to filamentous hyphal growth. We identified two genes needed for growth on GlcNAc (RON1 and NGS1) and found that mutants lacking these genes fail to induce the genes needed for GlcNAc catabolism. NGS1 was also important for growth on other sugars, such as maltose, but RON1 appeared to be specific for GlcNAc. Both mutants could grow on nonfermentable carbon sources indicating that they do not affect mitochondrial function, which we show is important for growth on GlcNAc but not for GlcNAc induction of hyphal morphogenesis. Interestingly, both the ron1D and ngs1D mutants were defective in forming hyphae in response to GlcNAc, even though GlcNAc catabolism is not required for induction of hyphal morphogenesis. The ron1D mutant showed a partial defect in forming hyphae, which was surprising since it displayed an elevated level of filamentous cells under noninducing conditions. The ron1D mutant also displayed an elevated basal level of expression of genes that are normally upregulated during hyphal growth. Consistent with this, Ron1 contains an Ndt80-like DNA-binding domain, indicating that it regulates gene expression. Thus, Ron1 is a key new component of the GlcNAc response pathway that acts as both an activator and a repressor of hyphal morphogenesis.

show abstract

“…N-Acetylglucosamine (GlcNAc) is another host environmental cue and a potent inducer of both filamentation and the opaque phenotype in C. albicans. GlcNAc functions primarily through the cAMP signaling pathway in the regulation of both filamentation and white-opaque switching (16,(19)(20)(21).…”

mentioning

confidence: 99%

pH Regulates White-Opaque Switching and Sexual Mating in Candida albicans

et al. 2015

View full text Add to dashboard Cite

bAs a successful commensal and pathogen of humans, Candida albicans encounters a wide range of environmental conditions. Among them, ambient pH, which changes frequently and affects many biological processes in this species, is an important factor, and the ability to adapt to pH changes is tightly linked with pathogenesis and morphogenesis. In this study, we report that pH has a profound effect on white-opaque switching and sexual mating in C. albicans. Acidic pH promotes white-to-opaque switching under certain culture conditions but represses sexual mating. The Rim101-mediated pH-sensing pathway is involved in the control of pH-regulated white-opaque switching and the mating response. Phr2 and Rim101 could play a major role in acidic pH-induced opaque cell formation. Despite the fact that the cyclic AMP (cAMP) signaling pathway does not play a major role in pH-regulated white-opaque switching and mating, white and opaque cells of the cyr1/cyr1 mutant, which is defective in the production of cAMP, showed distinct growth defects under acidic and alkaline conditions. We further discovered that acidic pH conditions repressed sexual mating due to the failure of activation of the Ste2-mediated ␣-pheromone response pathway in opaque a cells. The effects of pH changes on phenotypic switching and sexual mating could involve a balance of host adaptation and sexual reproduction in C. albicans.

show abstract

Novel roles for GlcNAc in cell signaling

Cited by 44 publications

References 33 publications

Control of chitin and N-acetylglucosamine utilization in Saccharopolyspora erythraea

Control of chitin and N-acetylglucosamine utilization in Saccharopolyspora erythraea

Regulation of Hyphal Growth and N-Acetylglucosamine Catabolism by Two Transcription Factors in Candida albicans

pH Regulates White-Opaque Switching and Sexual Mating in Candida albicans

Contact Info

Product

Resources

About