DNA 5-methylcytosine modification plays an important role in the regulation of a variety of biological functions in both prokaryotic and eukaryotic organisms. Previous studies show that DNA Cytosine-5-methylation is predominantly associated with restriction-modification system in bacteria. IPF4390 is deduced to be a putative type II DNA Cytosine-5 methyltransferase from a fresh water cyanobacterium, Microcystis aeruginosa. Both its substrate sequence specificity and catalytic mechanism need to be revealed. In this study, the cloning, expression, purification, DNA binding assays and crystallization of IPF4390 are reported. Results of DNA binding assays demonstrate that IPF4390 can specifically recognize and bind two double-stranded DNAs containing GGNCC (N = A, T, C or G) sequences (HgiBI: 5'-ATAAGGACCAATA-3'; TdeIII: 5'-ATAAGGGCCAATA-3'). Therefore, IPF4390 is probably capable of blocking endonuclease cleavage once restriction sites containing these sequences. Moreover, the crystal of IPF4390 in the presence of TdeIII was obtained, and its X-ray diffraction data were collected and scaled to a maximum resolution of 2.46 Å.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.pep.2021.105988 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A novel peptide CP29L, selected from the phage displayed cyclic random heptapeptide library, demonstrates its potent inhibitory effects to liver cancer HCCLM3 cells by targeting FOXM1.
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.
View Article and Find Full Text PDFRole of TRIM29 in disease: What is and is not known.
Int Immunopharmacol
January 2025
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 PDFA sensitive electrochemical DNA biosensor for detecting the genome of a plant growth-promoting bacteria.
Talanta
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 PDFAssignment of the N-terminal domain of mouse cGAS.
Biomol NMR Assign
January 2025
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 PDFMolecular and computational analysis of a novel pathogenic variant in emopamil-binding protein (EBP) involved in cholesterol biosynthetic pathway causing a rare male EBP disorder with neurologic defects (MEND syndrome).
Mol Biol Rep
January 2025
Department of Neuromuscular Disorders, UCL Queen Square Institute of Neurology, Queen Square House, London, WC1N 3BG, UK.
Background: Male EBP disorder with neurologic defects (MEND syndrome) is an extremely rare disorder with a prevalence of less than 1/1,000,000 individuals worldwide. It is inherited as an X-linked recessive disorder caused by impaired sterol biosynthesis due to nonmosaic hypomorphic EBP variants. MEND syndrome is characterized by variable clinical manifestations including intellectual disability, short stature, scoliosis, digital abnormalities, cataracts, and dermatologic abnormalities.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!