Biomedical subjects

Adelina Prado

Publications and source records attributed to Adelina Prado.

5 recordsLinked to original sources

PubMed2006

Sperm nuclear basic proteins of two closely related species of Scorpaeniform fish (Sebastes maliger, Sebastolobus sp.) with different sexual reproduction and the evolution of fish protamines.

In this paper, we present a review of sperm nuclear basic proteins (SNBPs) in teleost fish. The distribution of the three basic groups of SNBPs [histone (H)-type, protamine-like (PL)-type and protamine (P)-type], their evolution and possible relation to the mode of fertilization are described. In this regard, we have characterized the SNBPs from two closely related species of Scorpaeniform fish: internally fertilizing Sebastes maliger and externally fertilizing Sebastolobus sp., both in the family Scorpaenidae. Despite the different reproductive behavior of these two closely related rockfish species, in both instances the SNBP consists of protamines. However, there is a significant increase in the arginine content of the protamine in the internally fertilizing rockfish. The relevance of this observation is discussed within the context of the P-type SNBP in teleosts. The rapid evolution of teleost protamines, including those in rockfish, has also allowed us to obtain a molecular phylogeny for this group of bony fish that is almost indistinguishable from that currently available from the use of conventional anatomical/paleontological markers.

Amino Acid Sequence↗

PubMed2005

Nucleoplasmin-mediated unfolding of chromatin involves the displacement of linker-associated chromatin proteins.

We have previously characterized the interaction of nucleoplasmin with core histones and studied the possible involvement of this chaperone molecule in transcription. Here we study the interaction of nucleoplasmin with chromatin. We show that highly phosphorylated Xenopus laevis egg nucleoplasmin can unfold sperm and somatic chromatin in a way that involves the removal of chromosomal proteins from linker DNA regions without a stable interaction with the nucleosome. The complexes between egg nucleoplasmin and both somatic and sperm-specific linker proteins have been hydrodynamically characterized using sedimentation equilibrium in the analytical ultracentrifuge. The results are discussed within the context of the possible implication of nucleoplasmin in processes such as transcription and replication licensing which take place after egg fertilization at the onset of development.

Animals↗

PubMed2004

Nucleoplasmin: a nuclear chaperone.

In this article, we briefly review the structural and functional information currently available on nucleoplasmin. Special emphasis is placed on the discussion of the molecular mechanism involved in the sperm chromatin remodelling activity of this protein. A model is proposed based on current crystallographic data, recent biophysical and functional studies, as well as in the previously available information.

Active Transport, Cell Nucleus↗

PubMed2003

Activation mechanism of the nuclear chaperone nucleoplasmin: role of the core domain.

Nucleoplasmin (NP) mediates nucleosome assembly by removing basic proteins from sperm chromatin and exchanging them with histones. This function is modulated by phosphorylation of NP at multiple sites. NP is pentameric, each monomer consisting of two domains: a core, which forms a stable ring-like pentamer, and a tail, that holds a polyglutamic tract and the nuclear localization signal. In the present study, we have explored the role of the core domain in the functionality of NP. Despite lacking the poly-Glu region, a putative binding site for basic proteins, the isolated core domain of the hyperphosphorylated protein isolated from eggs of Xenopus laevis is able to bind sperm basic proteins and decondense chromatin, in contrast to the inactive, non-phosphorylated recombinant core. This activity can be reproduced artificially in the recombinant core domain through mutation of putative phosphorylation sites to aspartate, thus mimicking the charge effect of phosphorylation. The mutated residues locate in flexible or loop regions exposed on the "distal face" of the core pentamer, where a short acidic region is also found, indicating that phosphorylation might activate the core domain of NP by generating a strong localized negative potential. Our results show that the phosphorylated core domain of NP is active in chromatin decondensation, thus it could contribute together with the poly-Glu containing tail in displaying a binding surface for sperm basic proteins on the NP pentamer.

Animals↗

PubMed2002

Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity.

The chromatin decondensation activity, thermal stability, and secondary structure of recombinant nucleoplasmin, of two deletion mutants, and of the protein isolated from Xenopus oocytes have been characterized. As previously reported, the chromatin decondensation activity of recombinant, unphosphorylated nucleoplasmin is almost negligible. Our data show that deletion of 50 residues at the C-terminal domain of the protein, containing the positively charged nuclear localization sequence, activates its chromatin decondensation ability and decreases its stability. Interestingly, both the decondensation activity and thermal stability of this deletion mutant resemble those of the phosphorylated protein isolated from Xenopus oocytes. Deletion of 80 residues at the C-terminal domain, containing the above-mentioned positively charged region and a poly(Glu) tract, inactivates the protein and increases its thermal stability. These findings, along with the effect of salt on the thermal stability of these proteins, suggest that electrostatic interactions between the positive nuclear localization sequence and the poly(Glu) tract, at the C-terminal domain, modulate protein activity and stability.

Amino Acid Sequence↗