New insights into alterations in pl proteins affecting their binding to dna after exposure of mytilus galloprovincialis to mercury—a possible risk to sperm chromatin structure?

Autor: Antonella Giarra, Caterina Manna, Rosaria Notariale, Marco Trifuoggi, Marina Piscopo, Nadia Carusone, Gennaro Lettieri
Přispěvatelé: Lettieri, G., Notariale, R., Carusone, N., Giarra, A., Trifuoggi, M., Manna, C., Piscopo, M.
Jazyk: angličtina
Rok vydání: 2021
Předmět:
0301 basic medicine
Male
Turbidity assay
Water Pollutant
010501 environmental sciences
Protein aggregation
01 natural sciences
chemistry.chemical_compound
PL protein
Biology (General)
Fluorescence spectroscopy
Cell Nucleu
turbidity assays
Spectroscopy
Spectrum Analysi
Gel electrophoresis
biology
Chemistry
Reproduction
General Medicine
Spermatozoa
Mytilus
Chromatin
Computer Science Applications
Biochemistry
Mercuric Chloride
QH301-705.5
PL proteins
Sodium
HgCl
DNA-Binding Protein
chemistry.chemical_element
Catalysis
Inorganic Chemistry
03 medical and health sciences
HgCl2
Seawater
Physical and Theoretical Chemistry
QD1-999
Molecular Biology
0105 earth and related environmental sciences
Animal
Organic Chemistry
Mercury
biology.organism_classification
Sperm
030104 developmental biology
Sperm nuclei
Turbidimetry
Mussel
DNA
Zdroj: International Journal of Molecular Sciences
Volume 22
Issue 11
International Journal of Molecular Sciences, Vol 22, Iss 5893, p 5893 (2021)
Popis: Mercury (Hg) is a highly toxic and widespread pollutant. We previously reported that the exposure of Mytilus galloprovincialis for 24 h to doses of HgCl2 similar to those found in seawater (range 1–100 pM) produced alterations in the properties of protamine-like (PL) proteins that rendered them unable to bind and protect DNA from oxidative damage. In the present work, to deepen our studies, we analyzed PL proteins by turbidimetry and fluorescence spectroscopy and performed salt-induced release analyses of these proteins from sperm nuclei after the exposure of mussels to HgCl2 at the same doses. Turbidity assays indicated that mercury, at these doses, induced PL protein aggregates, whereas fluorescence spectroscopy measurements showed mercury-induced conformational changes. Indeed, the mobility of the PLII band changed in sodium dodecyl sulphate-polyacrylamide gel electrophoresis, particularly after exposure to 10-pM HgCl2, confirming the mercury-induced structural rearrangement. Finally, exposure to HgCl2 at all doses produced alterations in PL-DNA binding, detectable by DNA absorption spectra after the PL protein addition and by a decreased release of PLII and PLIII from the sperm nuclei. In conclusion, in this paper, we reported Hg-induced PL protein alterations that could adversely affect mussel reproductive activity, providing an insight into the molecular mechanism of Hg-related infertility.
Databáze: OpenAIRE
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