The Carbohydrate Metabolism of Lactiplantibacillus plantarum

Lactiplantibacillus plantarum has a strong carbohydrate utilization ability. This characteristic plays an important role in its gastrointestinal tract colonization and probiotic effects. L. plantarum LP-F1 presents a high carbohydrate utilization capacity. The genome analysis of 165 L. plantarum strains indicated the species has a plenty of carbohydrate metabolism genes, presenting a strain specificity. Furthermore, two-component systems (TCSs) analysis revealed that the species has more TCSs than other lactic acid bacteria, and the distribution of TCS also shows the strain specificity. In order to clarify the sugar metabolism mechanism under different carbohydrate fermentation conditions, the expressions of 27 carbohydrate metabolism genes, catabolite control protein A (CcpA) gene ccpA, and TCSs genes were analyzed by quantitative real-time PCR technology. The correlation analysis between the expressions of regulatory genes and sugar metabolism genes showed that some regulatory genes were correlated with most of the sugar metabolism genes, suggesting that some TCSs might be involved in the regulation of sugar metabolism.

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Identification of a Gene Cluster Enabling Lactobacillus casei BL23 To Utilize myo-Inositol

Applied and Environmental Microbiology ◽

10.1128/aem.00243-07 ◽

2007 ◽

Vol 73 (12) ◽

pp. 3850-3858 ◽

Cited By ~ 51

Author(s):

Marï¿½a Jesï¿½s Yebra ◽

Manuel Zï¿½ï¿½iga ◽

Sophie Beaufils ◽

Gaspar Pï¿½rez-Martï¿½nez ◽

Josef Deutscher ◽

...

Keyword(s):

Lactobacillus Casei ◽

Protein A ◽

Transcriptional Repressor ◽

Catabolic Pathway ◽

Gene Encoding ◽

Carbohydrate Utilization ◽

Alternative Pathways ◽

Semialdehyde Dehydrogenase ◽

Catabolite Control Protein A ◽

Dna Insertion

ABSTRACT Genome analysis of Lactobacillus casei BL23 revealed that, compared to L. casei ATCC 334, it carries a 12.8-kb DNA insertion containing genes involved in the catabolism of the cyclic polyol myo-inositol (MI). Indeed, L. casei ATCC 334 does not ferment MI, whereas strain BL23 is able to utilize this carbon source. The inserted DNA consists of an iolR gene encoding a DeoR family transcriptional repressor and a divergently transcribed iolTABCDG1G2EJK operon, encoding a complete MI catabolic pathway, in which the iolK gene probably codes for a malonate semialdehyde decarboxylase. The presence of iolK suggests that L. casei has two alternative pathways for the metabolism of malonic semialdehyde: (i) the classical MI catabolic pathway in which IolA (malonate semialdehyde dehydrogenase) catalyzes the formation of acetyl-coenzyme A from malonic semialdehyde and (ii) the conversion of malonic semialdehyde to acetaldehyde catalyzed by the product of iolK. The function of the iol genes was verified by the disruption of iolA, iolT, and iolD, which provided MI-negative strains. By contrast, the disruption of iolK resulted in a strain with no obvious defect in MI utilization. Transcriptional analyses conducted with different mutant strains showed that the iolTABCDG1G2EJK cluster is regulated by substrate-specific induction mediated by the inactivation of the transcriptional repressor IolR and by carbon catabolite repression mediated by the catabolite control protein A (CcpA). This is the first example of an operon for MI utilization in lactic acid bacteria and illustrates the versatility of carbohydrate utilization in L. casei BL23.

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Catabolite Control Protein A (CcpA) Contributes to Virulence and Regulation of Sugar Metabolism in Streptococcus pneumoniae

Journal of Bacteriology ◽

10.1128/jb.187.24.8340-8349.2005 ◽

2005 ◽

Vol 187 (24) ◽

pp. 8340-8349 ◽

Cited By ~ 127

Author(s):

Ramkumar Iyer ◽

Nitin S. Baliga ◽

Andrew Camilli

Keyword(s):

Streptococcus Pneumoniae ◽

Protein A ◽

Sugar Metabolism ◽

Invasive Disease ◽

Sugar Uptake ◽

Catabolite Control Protein A ◽

Control Protein ◽

Catabolite Control

ABSTRACT We characterized the role of catabolite control protein A (ccpA) in the physiology and virulence of Streptococcus pneumoniae. S. pneumoniae has a large percentage of its genome devoted to sugar uptake and metabolism, and therefore, regulation of these processes is likely to be crucial for fitness in the nasopharynx and may play a role during invasive disease. In many bacteria, carbon catabolite repression (CCR) is central to such regulation, influencing hierarchical sugar utilization and growth rates. CcpA is the major transcriptional regulator in CCR in several gram-positive bacteria. We show that CcpA functions in CCR of lactose-inducible β-galactosidase activity in S. pneumoniae. CCR of maltose-inducible α-glucosidase, raffinose-inducible α-galactosidase, and cellobiose-inducible β-glucosidase is unaffected in the ccpA strain, suggesting that other regulators, possibly redundant with CcpA, control these systems. The ccpA strain is severely attenuated for nasopharyngeal colonization and lung infection in the mouse, establishing its role in fitness on these mucosal surfaces. Comparison of the cell wall fraction of the ccpA and wild-type strains shows that CcpA regulates many proteins in this compartment that are involved in central and intermediary metabolism, a subset of which are required for survival and multiplication in vivo. Both in vitro and in vivo defects were complemented by providing ccpA in trans. Our results demonstrate that CcpA, though not a global regulator of CCR in S. pneumoniae, is required for colonization of the nasopharynx and survival and multiplication in the lung.

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Catabolite control protein a of Streptococcus suis type 2 contributes to sugar metabolism and virulence

The Journal of Microbiology ◽

10.1007/s12275-012-2035-3 ◽

2012 ◽

Vol 50 (6) ◽

pp. 994-1002 ◽

Cited By ~ 17

Author(s):

Yulong Tang ◽

Wei Wu ◽

Xiaoyan Zhang ◽

Zhongyan Lu ◽

Jianshun Chen ◽

...

Keyword(s):

Protein A ◽

Sugar Metabolism ◽

Streptococcus Suis ◽

Catabolite Control Protein A ◽

Control Protein ◽

Catabolite Control

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Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation

Molecular Microbiology ◽

10.1046/j.1365-2958.2002.03034.x ◽

2002 ◽

Vol 45 (2) ◽

pp. 543-553 ◽

Cited By ~ 70

Author(s):

Holger Ludwig ◽

Nicole Rebhan ◽

Hans-Matti Blencke ◽

Matthias Merzbacher ◽

Jorg Stulke

Keyword(s):

Bacillus Subtilis ◽

Protein A ◽

Catabolite Control Protein A ◽

Control Protein ◽

Catabolite Control

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Carbohydrate metabolism genes and pathways in insects: insights from the honey bee genome

Insect Molecular Biology ◽

10.1111/j.1365-2583.2006.00677.x ◽

2006 ◽

Vol 15 (5) ◽

pp. 563-576 ◽

Cited By ~ 84

Author(s):

T. Kunieda ◽

T. Fujiyuki ◽

R. Kucharski ◽

S. Foret ◽

S. A. Ament ◽

...

Keyword(s):

Carbohydrate Metabolism ◽

Honey Bee ◽

Carbohydrate Metabolism Genes

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SUN-PP040: Hypoxia-Induced Expression of Carbohydrate Metabolism Genes is Enhanced by Dietary Citric Acid

Clinical Nutrition ◽

10.1016/s0261-5614(15)30191-6 ◽

2015 ◽

Vol 34 ◽

pp. S38

Author(s):

Y. Hara ◽

N. Watanabe

Keyword(s):

Citric Acid ◽

Carbohydrate Metabolism ◽

Induced Expression ◽

Carbohydrate Metabolism Genes

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Alternative Lactose Catabolic Pathway in Lactococcus lactis IL1403

Applied and Environmental Microbiology ◽

10.1128/aem.71.10.6060-6069.2005 ◽

2005 ◽

Vol 71 (10) ◽

pp. 6060-6069 ◽

Cited By ~ 26

Author(s):

Tamara Aleksandrzak-Piekarczyk ◽

Jan Kok ◽

Pierre Renault ◽

Jacek Bardowski

Keyword(s):

Lactococcus Lactis ◽

Protein A ◽

Lactose Hydrolysis ◽

Galactosidase Activity ◽

Solid Media ◽

Pathway Gene ◽

Leloir Pathway ◽

Catabolite Control Protein A ◽

Lactis Il1403 ◽

Strong Control

ABSTRACT In this study, we present a glimpse of the diversity of Lactococcus lactis subsp. lactis IL1403 β-galactosidase phenotype-negative mutants isolated by negative selection on solid media containing cellobiose or lactose and X-Gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside), and we identify several genes essential for lactose assimilation. Among these are ccpA (encoding catabolite control protein A), bglS (encoding phospho-β-glucosidase), and several genes from the Leloir pathway gene cluster encoding proteins presumably essential for lactose metabolism. The functions of these genes were demonstrated by their disruption and testing of the growth of resultant mutants in lactose-containing media. By examining the ccpA and bglS mutants for phospho-β-galactosidase activity, we showed that expression of bglS is not under strong control of CcpA. Moreover, this analysis revealed that although BglS is homologous to a putative phospho-β-glucosidase, it also exhibits phospho-β-galactosidase activity and is the major enzyme in L. lactis IL1403 involved in lactose hydrolysis.

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NADP, corepressor for theBacilluscatabolite control protein CcpA

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.95.16.9590 ◽

1998 ◽

Vol 95 (16) ◽

pp. 9590-9595 ◽

Cited By ~ 57

Author(s):

Jeong-Ho Kim ◽

Martin I. Voskuil ◽

Glenn H. Chambliss

Keyword(s):

Dna Binding ◽

Binding Affinity ◽

Catabolite Repression ◽

Protein A ◽

Transcription Inhibition ◽

Gram Positive Bacteria ◽

Catabolite Control Protein A ◽

Dna Binding Affinity ◽

Reduced Forms ◽

Control Protein

Expression of the α-amylase gene (amyE) ofBacillus subtilisis subject to CcpA (catabolite control protein A)-mediated catabolite repression, a global regulatory mechanism inBacillusand other Gram-positive bacteria. To determine effectors of CcpA, we tested the ability of glycolytic metabolites, nucleotides, and cofactors to affect CcpA binding to theamyEoperator,amyO. Those that stimulated the DNA-binding affinity of CcpA were tested for their effect on transcription. HPr-P (Ser-46), proposed as an effector of CcpA, also was tested. In DNase I footprint assays, the affinity of CcpA foramyOwas stimulated 2-fold by fructose-1,6-diphosphate (FDP), 1.5-fold by oxidized or reduced forms of NADP, and 10-fold by HPr-P (Ser-46). However, the triple combinations, CcpA/NADP/HPr-P (Ser-46) and CcpA/FDP/HPr-P (Ser-46) synergistically stimulated DNA-binding affinity by 120- and 300-fold, respectively. NADP added to CcpA specifically stimulated transcription inhibition of theamyEpromoter by 120-fold. CcpA combined with HPr (Ser-46) inhibited transcription from theamyEpromoter, but it also inhibited several control promoters. FDP did not stimulate transcription inhibition by CcpA nor did the triple combinations. The finding that NADP had little effect on CcpA DNA binding but increased the ability of CcpA to inhibit transcription suggests that catabolite repression is not simply caused by CcpA bindingamyObut rather a result of interactions with the transcription machinery enhanced by NADP.

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Overexpressing MdFRK2-mediated Sugar Metabolism Accelerates Cellulose Accumulation in Apple and Poplar

10.21203/rs.3.rs-497881/v1 ◽

2021 ◽

Author(s):

Jing Su ◽

Chunxia Zhang ◽

Lingcheng Zhu ◽

Nanyang Yang ◽

Jingjing Yang ◽

...

Keyword(s):

Carbohydrate Metabolism ◽

Carbon Flux ◽

Sugar Metabolism ◽

Economic Benefits ◽

Phenotypic Traits ◽

Cellulose Synthesis ◽

Cellulose Content ◽

Common Component ◽

Photosynthetic Carbon ◽

New Strategy

Abstract Background: Cellulose is not only a common component in vascular plants, but also has great economic benefits for paper, wood, and industrial products. And its biosynthesis is highly regulated by carbohydrate metabolism and allocation in plant. MdFRK2, which encodes a key fructokinase (FRK) in apple, showed especially high affinity to fructose and regulated carbohydrate metabolism. Results: It was observed that overexpression of MdFRK2 in apple decreased sucrose (Suc) and fructose (Fru) with augmented FRK activity in stems, and caused the alterations of many phenotypic traits that include increased cellulose content and thickened primary phloem. To further investigate the involved mechanisms, we generated FRK2-OE poplar lines OE#1, OE#4 and OE#9 and discovered (1) a direct metabolic pathway for the biosynthesis of cellulose is that increased cleavage of Suc into UDP-glucose (UDPG) for cellulose synthesis via the increased sucrose synthase (SUSY) activity and transcript levels of PtrSUSY1, (2) another finding of this study is that overexpression of MdFRK2 resulted in the huge increased cellulose level by shifting the fructose 6-phosphate or glucose 6-phsophate towards UDPG formation, (3) that with increased UDPG in the sink tissue, and therefore more cellulose or hemicellulose can be used to thicker primary phloem. These results demonstrated that MdFRK2 overexpression would significantly changes the photosynthetic carbon flux from sucrose and hexose to UDPG for increased cellulose synthesis.Conclusions: The present data indicated that MdFRK2 overexpression in apple and poplar changes the photosynthetic carbon flux from sucrose and hexose to UDPG for stem cellulose synthesis. A new strategy is proposed to increase cellulose production by regulating sugar metabolism as a whole.

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