scholarly journals Role of ptsO in Carbon-Mediated Inhibition of the Pu Promoter Belonging to the pWW0Pseudomonas putida Plasmid

2001 ◽  
Vol 183 (17) ◽  
pp. 5128-5133 ◽  
Author(s):  
Ildefonso Cases ◽  
Francisco Velázquez ◽  
Vı́ctor de Lorenzo
Keyword(s):  
Gene Dosage ◽  
Sugar Transport ◽  
Regulatory Elements ◽  
Open Reading Frames ◽  
Type I ◽  
Phosphotransferase System ◽  
Wild Type Phenotype ◽  
Genomic Search ◽  
Regulatory Functions

ABSTRACT An investigation was made into the role of the ptsOgene in carbon source inhibition of the Pu promoter belonging to the Pseudomonas putida upper TOL (toluene degradation) operon. ptsO is coexpressed withptsN, the loss of which is known to renderPu unresponsive to glucose. Both ptsN andptsO, coding for the phosphoenolpyruvate:sugar phosphotransferase system (PTS) family proteins IIANtr and NPr, respectively, have been mapped adjacent to the rpoN gene of P. putida. The roles of these two genes in the responses of Pu to glucose were monitored by lacZ reporter technology with a P. putida strain engineered with all regulatory elements in monocopy gene dosage. In cells lacking ptsO,Pu activity seemed to be inhibited even in the absence of glucose. A functional relationship with ptsNwas revealed by the phenotype of a double ptsN ptsOmutant that was equivalent to the phenotype of a mutant with a singleptsN disruption. Moreover, phosphorylation of the product of ptsO seemed to be required for C inhibition of Pu, since an H15A change in the NPr sequence that prevents phosphorylation of this conserved amino acid residue did not restore the wild-type phenotype. A genomic search for proteins able to phosphorylate ptsO revealed the presence of two open reading frames, designated ptsP and mtp, with the potential to encode PTS type I enzymes in P. putida. However, neither an insertion in ptsPnor an insertion in mtp resulted in a detectable change in inhibition of Pu by glucose. These results indicate that some PTS proteins have regulatory functions in P. putida that are independent of their recognized role in sugar transport in other bacteria.

scholarly journals The Emerging Role of Long Non-Coding RNAs in Plant Defense Against Fungal Stress

2020 ◽  
Vol 21 (8) ◽  
pp. 2659
Author(s):  
Hong Zhang ◽  
Huan Guo ◽  
Weiguo Hu ◽  
Wanquan Ji
Keyword(s):  
Stress Responses ◽  
Higher Plants ◽  
Regulatory Elements ◽  
Cellular Functions ◽  
Non Coding Rna ◽  
Non Coding Rnas ◽  
Resistance To Infection ◽  
Regulatory Functions ◽  
Long Non Coding Rna

Growing interest and recent evidence have identified long non-coding RNA (lncRNA) as the potential regulatory elements for eukaryotes. LncRNAs can activate various transcriptional and post-transcriptional events that impact cellular functions though multiple regulatory functions. Recently, a large number of lncRNAs have also been identified in higher plants, and an understanding of their functional role in plant resistance to infection is just emerging. Here, we focus on their identification in crop plant, and discuss their potential regulatory functions and lncRNA-miRNA-mRNA network in plant pathogen stress responses, referring to possible examples in a model plant. The knowledge gained from a deeper understanding of this colossal special group of plant lncRNAs will help in the biotechnological improvement of crops.

scholarly journals Genetic evidence for the role of a bacterial phosphotransferase system in sugar transport.

1967 ◽  
Vol 58 (5) ◽  
pp. 1963-1970 ◽  
Author(s):  
R. D. Simoni ◽  
M. Levinthal ◽  
F. D. Kundig ◽  
W. Kundig ◽  
B. Anderson ◽  
...  
Keyword(s):  
Sugar Transport ◽  
Genetic Evidence ◽  
Phosphotransferase System ◽  
Bacterial Phosphotransferase System

scholarly journals Removal of a Membrane Anchor Reveals the Opposing Regulatory Functions ofVibrio choleraeGlucose-Specific Enzyme IIA in Biofilms and the Mammalian Intestine

mBio ◽  
2018 ◽  
Vol 9 (5) ◽  
Author(s):  
Vidhya Vijayakumar ◽  
Audrey S. Vanhove ◽  
Bradley S. Pickering ◽  
Julie Liao ◽  
Braden T. Tierney ◽  
...  
Keyword(s):  
Sugar Transport ◽  
Integral Membrane Protein ◽  
Amphipathic Helix ◽  
Specific Enzyme ◽  
Phosphotransferase System ◽  
Content Type ◽  
Protein Partners ◽  
And Behavior ◽  
Regulatory Functions ◽  
Mammalian Intestine

ABSTRACTTheVibrio choleraephosphoenolpyruvate phosphotransferase system (PTS) is a well-conserved, multicomponent phosphotransfer cascade that coordinates the bacterial response to carbohydrate availability through direct interactions of its components with protein targets. One such component, glucose-specific enzyme IIA (EIIAGlc), is a master regulator that coordinates bacterial metabolism, nutrient uptake, and behavior by direct interactions with cytoplasmic and membrane-associated protein partners. Here, we show that an amphipathic helix (AH) at the N terminus ofV. choleraeEIIAGlcserves as a membrane association domain that is dispensable for interactions with cytoplasmic partners but essential for regulation of integral membrane protein partners. By deleting this AH, we reveal previously unappreciated opposing regulatory functions for EIIAGlcat the membrane and in the cytoplasm and show that these opposing functions are active in the laboratory biofilm and the mammalian intestine. Phosphotransfer through the PTS proceeds in the absence of the EIIAGlcAH, while PTS-dependent sugar transport is blocked. This demonstrates that the AH couples phosphotransfer to sugar transport and refutes the paradigm of EIIAGlcas a simple phosphotransfer component in PTS-dependent transport. Our findings show thatVibrio choleraeEIIAGlc, a central regulator of pathogen metabolism, contributes to optimization of bacterial physiology by integrating metabolic cues arising from the cytoplasm with nutritional cues arising from the environment. Because pathogen carbon metabolism alters the intestinal environment, we propose that it may be manipulated to minimize the metabolic cost of intestinal infection.IMPORTANCETheV. choleraephosphoenolpyruvate phosphotransferase system (PTS) is a well-conserved, multicomponent phosphotransfer cascade that regulates cellular physiology and virulence in response to nutritional signals. Glucose-specific enzyme IIA (EIIAGlc), a component of the PTS, is a master regulator that coordinates bacterial metabolism, nutrient uptake, and behavior by direct interactions with protein partners. We show that an amphipathic helix (AH) at the N terminus ofV. choleraeEIIAGlcserves as a membrane association domain that is dispensable for interactions with cytoplasmic partners but essential for regulation of integral membrane protein partners. By removing this amphipathic helix, hidden, opposing roles for cytoplasmic partners of EIIAGlcin both biofilm formation and metabolism within the mammalian intestine are revealed. This study defines a novel paradigm for AH function in integrating opposing regulatory functions in the cytoplasm and at the bacterial cell membrane and highlights the PTS as a target for metabolic modulation of the intestinal environment.

Non-coding RNA-Encoded Peptides/Proteins in Human Cancer: The Future for Cancer Therapy

2021 ◽  
Vol 28 ◽  
Author(s):  
Seyedeh Zahra Bakhti ◽  
Saeid Latifi-Navid
Keyword(s):  
Cancer Metabolism ◽  
Human Cancer ◽  
Open Reading Frames ◽  
Clinical Value ◽  
Rna Transcripts ◽  
Non Coding Rna ◽  
Present Information ◽  
Regulatory Functions ◽  
Potential Use

: Although non-coding RNAs (ncRNAs) were initially thought to be a class of RNA transcripts with no encoding capability, it has been established that some ncRNAs actually contain open reading frames (ORFs), which can be translated into micropeptides or microproteins. Recent studies have reported that ncRNAs-derived micropeptides/microproteins have regulatory functions on various biological and oncological processes. Some of these micropeptides/microproteins act as tumor inhibitors and some as tumor inducers. Understanding the carcinogenic role of ncRNAs-encoded micropeptides/microproteins seems to pose potential challenges to cancer research and offer promising practical perspectives on cancer treatment. In this review, we summarized the present information on the association of ncRNAs-derived micropeptides/microproteins with different types of human cancers. We also mentioned their carcinogenic mechanisms in cancer metabolism, signaling pathways, cell proliferation, angiogenesis, metastasis, and so on. Finally, we discussed the potential clinical value of these micropeptides/microproteins and their potential use in the diagnosis and treatment of cancer. This information may help discover, optimize, and develop new tools based on biological micropeptides/microproteins for the early diagnosis and development of anticancer drugs.

scholarly journals How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

2006 ◽  
Vol 70 (4) ◽  
pp. 939-1031 ◽  
Author(s):  
Josef Deutscher ◽  
Christof Francke ◽  
Pieter W. Postma
Keyword(s):  
Protein Phosphorylation ◽  
Sugar Transport ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Phosphotransferase System ◽  
Nitrogen And Phosphorus ◽  
Coupling Energy ◽  
Catalytic Function ◽  
Sugar Derivatives ◽  
Regulatory Functions

SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

scholarly journals Genetic and Biochemical Characterization of the Phosphoenolpyruvate:Glucose/Mannose Phosphotransferase System of Streptococcus thermophilus

2003 ◽  
Vol 69 (9) ◽  
pp. 5423-5432 ◽  
Author(s):  
Armelle Cochu ◽  
Christian Vadeboncoeur ◽  
Sylvain Moineau ◽  
Michel Frenette
Keyword(s):  
Biochemical Characterization ◽  
Sugar Transport ◽  
Streptococcus Thermophilus ◽  
Phosphate Group ◽  
Phosphotransferase System ◽  
Whole Cells ◽  
Genes Encoding ◽  
Regulatory Functions

ABSTRACT In most streptococci, glucose is transported by the phosphoenolpyruvate (PEP):glucose/mannose phosphotransferase system (PTS) via HPr and IIABMan, two proteins involved in regulatory mechanisms. While most strains of Streptococcus thermophilus do not or poorly metabolize glucose, compelling evidence suggests that S. thermophilus possesses the genes that encode the glucose/mannose general and specific PTS proteins. The purposes of this study were to determine (i) whether these PTS genes are expressed, (ii) whether the PTS proteins encoded by these genes are able to transfer a phosphate group from PEP to glucose/mannose PTS substrates, and (iii) whether these proteins catalyze sugar transport. The pts operon is made up of the genes encoding HPr (ptsH) and enzyme I (EI) (ptsI), which are transcribed into a 0.6-kb ptsH mRNA and a 2.3-kb ptsHI mRNA. The specific glucose/mannose PTS proteins, IIABMan, IICMan, IIDMan, and the ManO protein, are encoded by manL, manM, manN, and manO, respectively, which make up the man operon. The man operon is transcribed into a single 3.5-kb mRNA. To assess the phosphotransfer competence of these PTS proteins, in vitro PEP-dependent phosphorylation experiments were conducted with purified HPr, EI, and IIABMan as well as membrane fragments containing IICMan and IIDMan. These PTS components efficiently transferred a phosphate group from PEP to glucose, mannose, 2-deoxyglucose, and (to a lesser extent) fructose, which are common streptococcal glucose/mannose PTS substrates. Whole cells were unable to catalyze the uptake of mannose and 2-deoxyglucose, demonstrating the inability of the S. thermophilus PTS proteins to operate as a proficient transport system. This inability to transport mannose and 2-deoxyglucose may be due to a defective IIC domain. We propose that in S. thermophilus, the general and specific glucose/mannose PTS proteins are not involved in glucose transport but might have regulatory functions associated with the phosphotransfer properties of HPr and IIABMan.

scholarly journals Phosphotransferase protein EIIANtr interacts with SpoT, a key enzyme of the stringent response, in Ralstonia eutropha H16

Microbiology ◽  
2014 ◽  
Vol 160 (4) ◽  
pp. 711-722 ◽  
Author(s):  
Katja Karstens ◽  
Christopher P. Zschiedrich ◽  
Botho Bowien ◽  
Jörg Stülke ◽  
Boris Görke
Keyword(s):  
Ralstonia Eutropha ◽  
Sugar Transport ◽  
Stringent Response ◽  
Nitrogen Deprivation ◽  
E Coli ◽  
Key Enzyme ◽  
Phosphoryl Groups ◽  
Regulatory Functions ◽  
Enzyme I

EIIANtr is a member of a truncated phosphotransferase (PTS) system that serves regulatory functions and exists in many Proteobacteria in addition to the sugar transport PTS. In Escherichia coli, EIIANtr regulates K+ homeostasis through interaction with the K+ transporter TrkA and sensor kinase KdpD. In the β-Proteobacterium Ralstonia eutropha H16, EIIANtr influences formation of the industrially important bioplastic poly(3-hydroxybutyrate) (PHB). PHB accumulation is controlled by the stringent response and induced under conditions of nitrogen deprivation. Knockout of EIIANtr increases the PHB content. In contrast, absence of enzyme I or HPr, which deliver phosphoryl groups to EIIANtr, has the opposite effect. To clarify the role of EIIANtr in PHB formation, we screened for interacting proteins that co-purify with Strep-tagged EIIANtr from R. eutropha cells. This approach identified the bifunctional ppGpp synthase/hydrolase SpoT1, a key enzyme of the stringent response. Two-hybrid and far-Western analyses confirmed the interaction and indicated that only non-phosphorylated EIIANtr interacts with SpoT1. Interestingly, this interaction does not occur between the corresponding proteins of E. coli. Vice versa, interaction of EIIANtr with KdpD appears to be absent in R. eutropha, although R. eutropha EIIANtr can perfectly substitute its homologue in E. coli in regulation of KdpD activity. Thus, interaction with KdpD might be an evolutionary ‘ancient’ task of EIIANtr that was subsequently replaced by interaction with SpoT1 in R. eutropha. In conclusion, EIIANtr might integrate information about nutritional status, as reflected by its phosphorylation state, into the stringent response, thereby controlling cellular PHB content in R. eutropha.

scholarly journals A Novel Role for Enzyme I of the Vibrio cholerae Phosphoenolpyruvate Phosphotransferase System in Regulation of Growth in a Biofilm

2007 ◽  
Vol 190 (1) ◽  
pp. 311-320 ◽  
Author(s):  
Laetitia Houot ◽  
Paula I. Watnick
Keyword(s):  
Vibrio Cholerae ◽  
Sugar Transport ◽  
Phosphotransferase System ◽  
Potent Inducer ◽  
Inducer Exclusion ◽  
Genes Encoding ◽  
Cell Components ◽  
Specific Regulation ◽  
Enzyme I

ABSTRACT Glucose is a universal energy source and a potent inducer of surface colonization for many microbial species. Highly efficient sugar assimilation pathways ensure successful competition for this preferred carbon source. One such pathway is the phosphoenolpyruvate phosphotransferase system (PTS), a multicomponent sugar transport system that phosphorylates the sugar as it enters the cell. Components required for transport of glucose through the PTS include enzyme I, histidine protein, enzyme IIAGlc, and enzyme IIBCGlc. In Escherichia coli, components of the PTS fulfill many regulatory roles, including regulation of nutrient scavenging and catabolism, chemotaxis, glycogen utilization, catabolite repression, and inducer exclusion. We previously observed that genes encoding the components of the Vibrio cholerae PTS were coregulated with the vps genes, which are required for synthesis of the biofilm matrix exopolysaccharide. In this work, we identify the PTS components required for transport of glucose and investigate the role of each of these components in regulation of biofilm formation. Our results establish a novel role for the phosphorylated form of enzyme I in specific regulation of biofilm-associated growth. As the PTS is highly conserved among bacteria, the enzyme I regulatory pathway may be relevant to a number of biofilm-based infections.

scholarly journals Impacts of uORF codon identity and position on translation regulation

2019 ◽  
Vol 47 (17) ◽  
pp. 9358-9367 ◽  
Author(s):  
Yizhu Lin ◽  
Gemma E May ◽  
Hunter Kready ◽  
Lauren Nazzaro ◽  
Mao Mao ◽  
...  
Keyword(s):  
Regulatory Elements ◽  
Open Reading Frames ◽  
Translation Regulation ◽  
Coding Region ◽  
Wide Range ◽  
Range Of Functions ◽  
Functional Peptides ◽  
Regulatory Functions ◽  
The Impact ◽  
Reading Frames

Abstract Translation regulation plays an important role in eukaryotic gene expression. Upstream open reading frames (uORFs) are potent regulatory elements located in 5′ mRNA transcript leaders. Translation of uORFs usually inhibit the translation of downstream main open reading frames, but some enhance expression. While a minority of uORFs encode conserved functional peptides, the coding regions of most uORFs are not conserved. Thus, the importance of uORF coding sequences on their regulatory functions remains largely unknown. We investigated the impact of an uORF coding region on gene regulation by assaying the functions of thousands of variants in the yeast YAP1 uORF. Varying uORF codons resulted in a wide range of functions, including repressing and enhancing expression of the downstream ORF. The presence of rare codons resulted in the most inhibitory YAP1 uORF variants. Inhibitory functions of such uORFs were abrogated by overexpression of complementary tRNA. Finally, regression analysis of our results indicated that both codon identity and position impact uORF function. Our results support a model in which a uORF coding sequence impacts its regulatory functions by altering the speed of uORF translation.

Role of phosphoenolpyruvate-phosphotransferase in glucose utilization by bacilli

1972 ◽  
Vol 182 (1067) ◽  
pp. 171-181 ◽  
Keyword(s):  
Bacillus Licheniformis ◽  
Glucose Utilization ◽  
Glycolytic Enzymes ◽  
Wild Type ◽  
Phosphotransferase System ◽  
Wild Type Phenotype

The growth of mutant Z4 of Bacillus licheniformis on glucose and on a number of other carbohydrates is impaired, but growth on fructose, glycerol and on glucuronate is not. There are no significant differences between the mutant and its parent in the levels of glycolytic enzymes and in the ability of the organisms to take up labelled fructose; in contrast, the mutant takes up and phosphorylates labelled glucose, and its analogues methyl α -glucoside and 2-deoxyglucose, to a much smaller extent than does the wild-type. Extracts of the mutant are virtually devoid of the inducible phosphoenolpyruvate-dependent glucose phosphotransferase present in the parent, though fructose phosphotransferase activity is present in both organisms. Revertants of Z4 , selected for growth on glucose, fully regain the wild-type phenotype. These results show that the phosphotransferase system plays a necessary role in the utilization of glucose by bacilli.

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