MSMEG_2295 is a TetR family protein encoded by the first gene of a (Msm) operon that expresses the gene for DinB2 (MSMEG_2294), a translesion DNA repair enzyme. We have carried out investigations to understand its function by performing DNA binding studies and gene knockout experiments. We found that the protein binds to a conserved inverted repeat sequence located upstream of the operon and several other genes. Using a knockout of , we show that MSMEG_2295 controls the expression of at least five genes, the products of which could potentially influence carbohydrate and fatty acid metabolism as well as antibiotic and oxidative stress resistance. We have demonstrated that MSMEG_2295 is a repressor by performing complementation analysis. Knocking out of had a significant impact on pyruvate metabolism. Pyruvate dehydrogenase activity was virtually undetectable in although in the complemented strain, it was high. We also show that knocking out of causes resistance to HO, reversed in the complemented strain. We have further found that the mycobacterial growth inhibitor plumbagin, a compound of plant origin, acts as an inducer of MSMEG_2295 regulated genes. We, therefore, establish that MSMEG_2295 functions by exerting its role as a repressor of multiple Msm genes and that by doing so, it plays a vital role in controlling pyruvate metabolism and response to oxidative stress.
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Eur J Pharmacol
January 2025
School of Life Science and Engineering, Southwest Jiaotong University, Chengdu 610031, Sichuan province, P.R. China. Electronic address:
FOXM1 is the "Achilles' heel" of cancers and hence the potential therapeutic target for anticancer drug discovery. In this work, we selected high affinity peptides against the protein of human DNA binding domain of FOXM1 (FOXM1-DBD) from the disulfide-constrained, phage displayed random cyclic heptapeptide library Ph.D.
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Key Laboratory of Livestock Infectious Diseases, Ministry of Education, Key Laboratory of Zoonosis, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, 120 Dongling Road, Shenyang 110866, China; The Research Unit for Pathogenic Mechanisms of Zoonotic Parasites, Chinese Academy of Medical Sciences, 120 Dongling Road, Shenyang 110866, China. Electronic address:
Tripartite motif-containing proteins (TRIMs), comprising the greatest subfamily of E3 ubiquitin ligases with approximately 80 members of this family, are widely distributed in mammalian cells. TRIMs actively participate in ubiquitination of target proteins, a type of post-translational modification associated with protein degradation and other functions. Tripartite motif-containing protein 29 (TRIM29), a member of the TRIM family, differs from other members of this family in that it lacks the RING finger structural domain containing cysteine and histidine residues that mediates DNA binding, protein-protein interactions, and ubiquitin ligase, at its N-terminus.
View Article and Find Full Text PDFTalanta
January 2025
Department of Chemistry, State University of Ponta Grossa, Ponta Grossa, CEP 84030-900, PR, Brazil. Electronic address:
The challenge of increasing food production while maintaining environmental sustainability can be addressed by using biofertilizers such as Azospirillum, which can enhance plant growth and colonize more than 100 plant species. The success of this biotechnology depends on the amount of plant growth-promoting bacteria associated with the plant during crop development. However, monitoring bacterial population dynamics after inoculation requires time-consuming, laborious, and costly procedures.
View Article and Find Full Text PDFBiomol NMR Assign
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Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Cyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete H, N, and C backbone chemical-shift assignments of mouse cGAS NTD (residues 5-146), obtained with a set of 3D and 4D solution NMR experiments.
View Article and Find Full Text PDFMol Biol Rep
January 2025
Department of Neuromuscular Disorders, UCL Queen Square Institute of Neurology, Queen Square House, London, WC1N 3BG, UK.
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