The interaction of the 16-mer synthetic peptide (Aβ16), which represents the metal-binding domain of the amyloid-β with DNA, was studied employing the surface plasmon resonance technique. It has been shown that Aβ16 binds to the duplex DNA in the presence of zinc ions and thus the metal-binding domain can serve as a zinc-dependent DNA-binding site of the amyloid-β. The interaction of Aβ16 with DNA most probably depends on oligomerization of the peptide and is dominated by interaction with phosphates of the DNA backbone.
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http://dx.doi.org/10.3233/JAD-130122 | DOI Listing |
Int J Mol Sci
November 2024
Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou 310029, China.
Cadmium (Cd) and lead (Pb) are the primary hazardous heavy metals that accumulate in crops and pose substantial risks to public health via the food chain. Limiting the migration of these toxic metals from contaminated environments to rice is the most direct and crucial remediation approach. Bioremediation with microorganisms has been extensively utilized for managing heavy metal contamination in the natural environment, and the interplay between microbes and crops is important to alleviate heavy metal stress.
View Article and Find Full Text PDFProtein Sci
January 2025
Departament de Genètica, Microbiologia i Estadística, Facultat de Biologia, Universitat de Barcelona (UB), Barcelona, Spain.
Protein modularity is acknowledged for promoting the emergence of new protein variants via domain rearrangements. Metallothioneins (MTs) offer an excellent model system for experimentally examining the consequences of domain rearrangements due to the possibility to assess the functional properties of native and artificially created variants using spectroscopic methods and metal tolerance assays. In this study, we have investigated the functional properties of AbiMT4 from the snail Alinda biplicata (Gastropoda, Mollusca), a large MT comprising 10 putative β domains (β3β1), alongside four artificially designed variants differing in domain number, type, or order.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
December 2024
Department of Ecology and Evolutionary Biology, University of Arizona, Tucson, AZ 85721.
The current "consensus" order in which amino acids were added to the genetic code is based on potentially biased criteria, such as the absence of sulfur-containing amino acids from the Urey-Miller experiment which lacked sulfur. More broadly, abiotic abundance might not reflect biotic abundance in the organisms in which the genetic code evolved. Here, we instead identify which protein domains date to the last universal common ancestor (LUCA) and then infer the order of recruitment from deviations of their ancestrally reconstructed amino acid frequencies from the still-ancient post-LUCA controls.
View Article and Find Full Text PDFBiochemistry
January 2025
Department of Chemistry, Vassar College, 124 Raymond Ave, Poughkeepsie, New York 12604, United States.
are often the most abundant, commensal species in the gut microbiome of industrialized human populations. One of the most commonly detected species is . It has been linked to benefits like the suppression of intestinal inflammation but is also correlated with some autoimmune disorders, for example irritable bowel disorder (IBD).
View Article and Find Full Text PDFCommun Biol
December 2024
School of Chemistry and Chemical Engineering, University of South China, Hengyang, China.
Allosteric conformational change is an important paradigm in the regulation of protein function, which is typically triggered by the binding of small cofactors, metal ions or protein partners. Here, we found those conformational transitions can be effectively monitored by F NMR, facilitated by a site-specific F incorporation strategy at the protein C-terminus using asparaginyl endopeptidase (AEP). Three case studies show that C-terminal F-nuclei can reveal protein dynamics not only adjacent but also distal to C-terminus, including those occurring in a hemoprotein neuroglobin (Ngb), calmodulin (CaM), and a cobalt metalloregulator (CoaR) responding to both cobalt and tetrapyrrole.
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