scholarly journals Effects of the overexpression of fructose-1,6-bisphosphate aldolase on fermentation pattern and transcription of the genes encoding lactate dehydrogenase and pyruvate formate-lyase in a ruminal bacterium, Streptococcus bovis

2004 ◽  
Vol 50 (2) ◽  
pp. 71-78 ◽  
Author(s):  
Narito Asanuma ◽  
Takahiro Yoshii ◽  
Masahiro Kikuchi ◽  
Tsuneo Hino
Keyword(s):  
Lactate Dehydrogenase ◽  
Ruminal Bacterium ◽  
Streptococcus Bovis ◽  
Pyruvate Formate Lyase ◽  
Genes Encoding ◽  
Fermentation Pattern ◽  
Fructose 1,6 Bisphosphate

scholarly journals Molecular Characterization of CcpA and Involvement of This Protein in Transcriptional Regulation of Lactate Dehydrogenase and Pyruvate Formate-Lyase in the Ruminal Bacterium Streptococcus bovis

2004 ◽  
Vol 70 (9) ◽  
pp. 5244-5251 ◽  
Author(s):  
Narito Asanuma ◽  
Takahiro Yoshii ◽  
Tsuneo Hino
Keyword(s):  
Lactate Dehydrogenase ◽  
Transcriptional Control ◽  
Mrna Level ◽  
Protein A ◽  
Streptococcus Bovis ◽  
Pyruvate Formate Lyase ◽  
Catabolite Control Protein A ◽  
Responsive Element ◽  
Fructose 1,6 Bisphosphate

ABSTRACT A ccpA gene that encodes global catabolite control protein A (CcpA) in Streptococcus bovis was identified and characterized, and the involvement of CcpA in transcriptional control of a gene (ldh) encoding lactate dehydrogenase (LDH) and a gene (pfl) encoding pyruvate formate-lyase (PFL) was examined. The ccpA gene was shown to be transcribed as a monocistronic operon. A catabolite-responsive element (cre) was found in the promoter region of ccpA, suggesting that ccpA transcription in S. bovis is autogenously regulated. CcpA required HPr that was phosphorylated at the serine residue at position 46 (HPr-[Ser-P]) for binding to the cre site, but glucose 6-phosphate, fructose 1,6-bisphosphate, and NADP had no effect on binding. Diauxic growth was observed when S. bovis was grown in a medium containing glucose and lactose, but it disappeared when ccpA was disrupted, which indicates that CcpA is involved in catabolite repression in S. bovis. The level of ccpA mRNA was higher when cells were grown on glucose than when they were grown on lactose, which was in line with the level of ldh mRNA. When cells were grown on glucose, the ldh mRNA level was lower but the pfl mRNA level was higher in a ccpA-disrupted mutant than in the parent strain, which suggests that ldh transcription is enhanced and pfl transcription is suppressed by CcpA. The ccpA-disrupted mutant produced less lactate and more formate than the parent, probably because the mutant had reduced LDH activity and elevated PFL activity. In the upper region of both ldh and pfl, a cre-like sequence was found, suggesting that the complex consisting of CcpA and HPr-[Ser-P] binds to the possible cre sites. Thus, CcpA appears to be involved in the global regulation of sugar utilization in S. bovis.

scholarly journals Regulation of CcpA on the growth and organic acid production characteristics of ruminal Streptococcus bovis at different pH

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Yaqian Jin ◽  
Chao Wang ◽  
Yaotian Fan ◽  
Mawda Elmhadi ◽  
Ying Zhang ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Type Strain ◽  
Significant Interaction ◽  
Wild Type Strain ◽  
Acetate Kinase ◽  
Wild Type ◽  
Pyruvate Formate Lyase ◽  
Relative Expression ◽  
Knockout Strain ◽  
Fermentation Pattern

Abstract Background Catabolite control protein A (CcpA) regulates the transcription of lactate dehydrogenase and pyruvate formate-lyase in Streptococcus bovis, but knowledge of its role in response to different pH is still limited. In this study, a ccpA-knockout strain of S. bovis S1 was constructed and then used to examine the effects of ccpA gene deletion on the growth and fermentation characteristics of S. bovis S1 at pH 5.5 or 6.5. Results There was a significant interaction between strain and pH for the maximum specific growth rate (μmax) and growth lag period (λ), which caused a lowest μmax and a longest λ in ccpA-knockout strain at pH 5.5. Deletion of ccpA decreased the concentration and molar percentage of lactic acid, while increased those of formic acid. Strains at pH 5.5 had decreased concentrations of lactic acid and formic acid compared to pH 6.5. The significant interaction between strain and pH caused the highest production of total organic acids and acetic acid in ccpA-knockout strain at pH 6.5. The activities of α-amylase and lactate dehydrogenase decreased in ccpA-knockout strain compared to the wild-type strain, and increased at pH 5.5 compared to pH 6.5. There was a significant interaction between strain and pH for the activity of acetate kinase, which was the highest in the ccpA-knockout strain at pH 6.5. The expression of pyruvate formate-lyase and acetate kinase was higher in the ccpA-knockout strain compared to wild-type strain. The lower pH improved the relative expression of pyruvate formate-lyase, while had no effect on the relative expression of acetate kinase. The strain × pH interaction was significant for the relative expression of lactate dehydrogenase and α-amylase, both of which were highest in the wild-type strain at pH 5.5 and lowest in the ccpA-knockout strain at pH 6.5. Conclusions Overall, low pH inhibited the growth of S. bovis S1, but did not affect the fermentation pattern. CcpA regulated S. bovis S1 growth and organic acid fermentation pattern. Moreover, there seemed to be an interaction effect between pH and ccpA deletion on regulating the growth and organic acids production of S. bovis S1.

scholarly journals Molecular Characterization and Expression of Pyruvate Formate-Lyase-Activating Enzyme in a Ruminal Bacterium, Streptococcus bovis

2002 ◽  
Vol 68 (7) ◽  
pp. 3352-3357 ◽  
Author(s):  
Narito Asanuma ◽  
Tsuneo Hino
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Mrna Level ◽  
Lactate Production ◽  
Growth Conditions ◽  
Ruminal Bacterium ◽  
Streptococcus Bovis ◽  
Gene Encoding ◽  
Pyruvate Formate Lyase ◽  
Ldh Activity

ABSTRACT To clarify the significance of the activation of pyruvate formate-lyase (PFL) by PFL-activating enzyme (PFL-AE) in Streptococcus bovis, the molecular properties and gene expression of PFL-AE were investigated. S. bovis PFL-AE was deduced to consist of 261 amino acids with a molecular mass of 29.9 kDa and appeared to be a monomer protein. Similar to Escherichia coli PFL-AE, S. bovis PFL-AE required Fe2+ for activity. The gene encoding PFL-AE (act) was found to be polycistronic, and the PFL gene (pfl) was not included. However, the act mRNA level changed in parallel with the pfl mRNA level, responding to growth conditions, and the change was contrary to the change in the lactate dehydrogenase (LDH) mRNA level. PFL-AE synthesis appeared to change in parallel with PFL synthesis. Introduction of a recombinant plasmid containing S. bovis pfl and the pfl promoter into S. bovis did not affect formate and lactate production, which suggests that the activity of the pfl promoter is low. When the pfl promoter was replaced by the S. bovis ldh promoter, PFL was overexpressed, which caused an increase in the formate-to-lactate ratio. However, when PFL-AE was overexpressed, the formate-to-lactate ratio did not change, suggesting that PFL-AE was present at a level that was high enough to activate PFL. When both PFL-AE and PFL were overexpressed, the formate-to-lactate ratio further increased. It is conceivable that LDH activity is much higher than PFL activity, which may explain why the formate-to-lactate ratio is usually low.

Inhibition of Rhizopus lactate dehydrogenase by fructose 1,6-bisphosphate

2009 ◽  
Vol 44 (4) ◽  
pp. 242-247 ◽  
Author(s):  
Christopher D. Skory ◽  
Jeffrey A. Mertens ◽  
Joseph O. Rich
Keyword(s):  
Lactate Dehydrogenase ◽  
Fructose 1,6 Bisphosphate

ATPase-dependent energy spilling by the ruminal bacterium, Streptococcus bovis

1990 ◽  
Vol 153 (4) ◽  
pp. 378-383 ◽  
Author(s):  
James B. Russell ◽  
Herbert J. Strobel
Keyword(s):  
Ruminal Bacterium ◽  
Streptococcus Bovis ◽  
Energy Spilling
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