Our findings offer a novel molecular understanding of nucleoplasmin in sperm chromatin decondensation and subsequent developmental chromatin reprogramming at individual molecular level.Ĭhromatin remodeling DNA condensation Decondensation Magnetic tweezers Nucleoplasmin.Ĭopyright © 2018 Elsevier B.V. These observations imply that the chaperone effects of nucleoplasmin during the decondensation/condensation process may be driven by specific spatial configuration of its acidic pentamer structure, rather than by electrostatic interaction. In contrast, nucleoplasmin is able to assist the histone transfer process, even though it carries the same negative charge as RNA and polyglutamic acid. After decondensation, both RNA and polyglutamic acid prevented the transfer of histones onto the naked DNA. The affinity binding of the different polyanions with protamine suggests chaperone-mediated chromatin decondensation activity occurs through protein-protein interactions. In addition to nucleoplasmin, 53BP1 (TP53-binding protein 1) also has a classical BP NLS with the sequence 1666 GKRKLITSEEERSPAKRGRKS 1686. Once DNA was condensed, nucleoplasmin, polyglutamic acid, and RNA could remove protamine from the DNA at different rates. For instance, the BP NLS at the C-terminus of nucleoplasmin, whose sequence is 155 KRPAATKKAGQAKKKK 170, can guide the protein into the nucleus. We found that protamine induces DNA condensation in a stepwise manner. Herein, magnetic tweezers (MT) and a chromatin assembly system were used to study the nucleoplasmin-mediated DNA decondensation/condensation at the single-molecular level in vitro. However, knowledge on nucleoplasmin in chromatin formation remains elusive. Nucleoplasmin is a key factor in regulating nucleosome assembly as a chaperone during fertilization process. Fertilization requires decondensation of promatine-condensed sperm chromatin, a dynamic process serving as an attractive system for the study of chromatin reprogramming.
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