Protamine-like proteins (PL-II, PL-III and PL-IV) represent the major basic nuclear component of Mytilus galloprovincialis L sperm chromatin. The present study investigates the effects induced on the properties of PL-II protein after exposure of Mytilus galloprovincialis L for 24 h to 1.5 and 5 mu M CdCl2. We found cadmium accumulation in protamine-like proteins with a linear grow up with the exposition dose. In particular, after 5 mu M CdCl2 mussels exposure, the mobility of PL-II band changed in SDS-PAGE, suggesting structural rearrangement in presence of cadmium. Structural analysis using fluorescent probes, indicated that at 5 mu M CdCl2 the complete conformational change of PL-II protein was reached. In the same condition of mussels exposure of 5 mu M CdCl2, PL-II protein changed its DNA binding mode, which determined a closer DNA binding, because higher amount of NaCl were required for PL-II protein release by sperm nuclei. These results supported the hypothesis that mussel exposure to this CdCl2 dose, although lower to toxic ones, affects the properties of this protein and as a consequence chromatin organization of spermatozoa that is essential for the success of fertilization.

Alterations in the properties of sperm protamine-like II protein after exposure of Mytilus galloprovincialis (Lamarck 1819) to sub-toxic doses of cadmium

Febbraio Ferdinando;
2019

Abstract

Protamine-like proteins (PL-II, PL-III and PL-IV) represent the major basic nuclear component of Mytilus galloprovincialis L sperm chromatin. The present study investigates the effects induced on the properties of PL-II protein after exposure of Mytilus galloprovincialis L for 24 h to 1.5 and 5 mu M CdCl2. We found cadmium accumulation in protamine-like proteins with a linear grow up with the exposition dose. In particular, after 5 mu M CdCl2 mussels exposure, the mobility of PL-II band changed in SDS-PAGE, suggesting structural rearrangement in presence of cadmium. Structural analysis using fluorescent probes, indicated that at 5 mu M CdCl2 the complete conformational change of PL-II protein was reached. In the same condition of mussels exposure of 5 mu M CdCl2, PL-II protein changed its DNA binding mode, which determined a closer DNA binding, because higher amount of NaCl were required for PL-II protein release by sperm nuclei. These results supported the hypothesis that mussel exposure to this CdCl2 dose, although lower to toxic ones, affects the properties of this protein and as a consequence chromatin organization of spermatozoa that is essential for the success of fertilization.
2019
Istituto di Biochimica e Biologia Cellulare - IBBC
Cadmium
Mytilus galloprovincialis L.
Metal pollution
Sperm chromatin
Protamine-like proteins
Metal bioaccumulation
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/376427
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