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- Bioerosive structures of sclerozoan foraminifera from the lower pliocene of southern Spain: a contribution to the palaeoecology of marine hard substrate communitiesPublication . Santos, A; Mayoral, EA palaeoecological study of sclerozoan foraminifera of the families Saccamminidae (aff. Sagenina), Lituolidae (Placopsilina), Cibicididae (Cibicides, Dyocibicides, Cibicidella) and Planorbulinidae (Planorbulina and Planorbulinella) that colonized epifaunal bivalves (ostreids and pectinids) during the early Pliocene in southern Spain has led to the recognition of two new boring ichnogenera: Camarichnus ichnogen. nov., with two ichnospecies, C. subrectangularis ichnosp. nov. and C. arcuatus ichnosp. nov., and Canalichnus ichnogen. nov., with one ichnospecies, C. tenuis ichnosp. nov. The first two ichnospecies were produced by adnate lituolids and cibicidids, the last by saccamminids. Their recognition is very important when quantifying populations of these organisms. Colonisation took place after death of the host bivalves, when they acted as very stable substrates whose topography probably controlled the initial settlement pattern of the foraminifera. The colonisation sequence started with the foraminifera (lituolids-saccamminids-cibicidids-planorbulinids) and was followed by vermetid gastropods, serpulids, spirorbids, cheilostome bryozoans and/or ostreids. Preferred orientations and over-growth relationships between cheilostome bryozoans and serpulids have been detected in this material.
- Actomyosin modulation by peroxynitritePublication . Tiago, Teresa; Silva, D.; Santos, Ana; Aureliano, M.; Gutiérrez-Merino, CarlosIn the present work we address the oxidative modifications accounting for the structural and functional impairment of the actomyosin complex under the oxidative stress mediated by peroxynitrite (ONOO-). Experiments on purified myosin and actin have shown that submicromolar ONOO- concentrations produce strong inhibition of the F-actin stimulated myosin ATPase activity. The peroxynitrite-induced actomyosin impairment correlated with structural modifications that decrease the thermal stability of both actin and myosin leading to partially unfolded states. The results suggest a major role for the highly reactive cysteines on actin and on myosin and also for some critical methionines on G-actin. 3-nitrotyrosine does not contribute significantly to the observed functional alterations.