Artisanal shark fisheries have been an important source of food and employment in Mexico for many years. In the Gulf of Mexico, this multispecific fishery is based on the seasonal abundance of several shark and teleost species. To obtain fishery and biological information needed to manage the fishery and conserve shark stocks, intensive monitoring of artisanal shark landings was undertaken from November 1993 to December 1994. The State of Campeche had the highest landings and effort. October 1994 had the highest monthly catch per unit effort for all species and areas combined (27.2 sharks per trip). Rhizoprionodon terraenovae (46%), Sphyrna tiburo (15%), and Carcharhinus limbatus (11%) accounted for most of the landings numerically, and the highest catch per unit effort for C. limbatus occurred late in the year as a result of increased landings attributable to an annual southward migration from USA to Mexican waters. The high proportion of neonate and juvenile sharks in gill-net catches from shallow coastal waters suggests that the main shark nursery areas are under heavy fishing pressure. In light of the heavy exploitation of shark resources, the Mexican National Fisheries Institute recommends a number of precautionary actions to avoid the collapse of this fishery. Resumen. Las pesquerías artesanales de tiburones han sido una importante fuente de alimento y empleo en México durante muchos años. En el Golfo de México, esta pesquería multiespecífica está basada en la abundancia estacional de diversas especies de tiburones y peces. Para obtener la información biológico-pesquera necesaria para manejar la pesquería y conservar los stocks de tiburones, se realizó un monitoreo de las capturas artesanales de tiburón entre noviembre de 1993 y diciembre de 1994. Campeche presentó las mayores capturas y esfuerzo. En octubre de 1994 se registraron las mayores CPUE para todas las especies y áreas combinadas (27.2 tiburones por viaje). Rhizoprionodon terraenovae (46%), Sphyrna tiburo (15%) y Carcharhinus limbatus (11%) constituyeron la mayoría de las capturas numéricamente y las mayores CPUE para C. limbatus se produjeron hacia finales de año a consecuencia del aumento de las capturas atribuible a una migración anual norte-sur desde los E.U. hacia aguas mexicanas. La alta proporción de neonatos y juveniles capturados en redes agalleras en aguas costeras someras sugiere que las principales áreas de crianza están sometidas a una alta presión de pesca. En vista de los niveles de explotación el INP recomienda diversas medidas precautorias para evitar el colapso de la pesquería.

Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm chromatin and depositing H2A-H2B histone dimers. It has been proposed that histones could bind to either the lateral or distal face of the pentameric structure. Here, we combine different biochemical and biophysical techniques to show that natural, hyperphosphorylated NP can bind five H2A-H2B dimers and that the amount of bound ligand depends on the overall charge (phosphorylation level) of the chaperone. Three-dimensional reconstruction of NP/H2A-H2B complex carried out by electron microscopy reveals that histones interact with the chaperone distal face. Limited proteolysis and mass spectrometry indicate that the interaction results in protection of the histone fold and most of the H2A and H2B C-terminal tails. This structural information can help to understand the function of NP as a histone chaperone.

Fourier transform infrared spectroscopy, circular dichroism and prediction techniques have been used to investigate the conformational properties of nucleoplasmin isolated from oocytes and eggs of Xenopus. laevis and overexpressed in Escherichia coli. A simple and fast method allows purification of recombinant nucleoplasmin free of truncated and/or aggregated forms, and therefore provides a suitable sample to carry out the structural and functional comparison between these proteins. The secondary structure of the three proteins estimated from both spectroscopic techniques was very similar, and was found to be 31--33% loops, 27--34% beta structure, 22--26% turns and 9-14% alpha helix. Prediction studies, in good agreement with experimental data, also suggest that beta structure is the major regular conformation, and that loops and turns are the most abundant conformational features within the secondary structure of nucleoplasmin. Furthermore, the spectroscopic characterization of a truncated version of the protein, lacking 80 residues at the C-terminus, and the prediction data indicate that the secondary structure elements of the protein are segregated into two regions. The N-terminal fragment (comprising residues 1--120) which holds all the putative beta strands, and the solvent-exposed C-terminal region, that is suggested to be enriched in turn and loop structures. The phosphate/protein monomer molar ratios, obtained from chemical analysis and mass spectrometry, are 0, 3 and 7--10 for recombinant, oocyte and egg nucleoplasmin, respectively. Phosphorylation does not significantly affect the secondary structure of the protein, but clearly modulates its ability to decondense sperm nuclei and to remove basic proteins from DNA.

Nucleoplasmin (NP) is a histone chaperone involved in nucleosome assembly, chromatin decondensation at fertilization, and apoptosis. To carry out these activities NP has to interact with different types of histones, an interaction that is regulated by phosphorylation. Here we have identified a number of phosphorylated residues by mass spectrometry and generated mutants in which these amino acids are replaced by Asp to mimic the effect of phosphorylation. Our results show that, among the eight phosphoryl groups experimentally detected, four are located at the flexible N terminus, and the rest are found at the tail domain, flanking the nuclear localization signal. Phosphorylation-mimicking mutations render a recombinant protein as active in chromatin decondensation as hyperphosphorylated NP isolated from Xenopus laevis eggs. Comparison of mutants in which the core and tail domains of the protein were independently or simultaneously "activated" indicates that activation or phosphorylation of both protein domains is required for NP to efficiently extract linker-type histones from chromatin.