Monitoring of Dinophysis species and diarrhetic shellfish toxins in Flødevigen Bay, Norway: inter-annual variability over a 25-year time-series.

The accumulation of phycotoxins in bivalve mussels associated with mussels feeding on toxic phytoplankton is a well-known phenomenon in Norway. Regular monitoring for 25 years has revealed that accumulation of Diarrhetic Shellfish poisoning (DSP) toxins in mussels is the main phycotoxin problem along the Norwegian coast. The aim of this study was to evaluate possible trends over time of Dinophysis spp. and DSP as well as possible correlation between abundance of Dinophysis spp. and toxin accumulation in mussels, as based on intensive and regular monitoring at the southern coast of Norway at Flødevigen Bay. The main source organism causing a risk of DSP in Norway is Dinophysis acuta. However, it cannot be excluded that other Dinophysis spp., e.g. D. acuminata and D. norvegica, may contribute to the total accumulation of toxins. The variability in the occurrence of these species is high at both short- and long-term; between days and between years. There are, however, some important overall patterns in the occurrence of the species during the last decades. Dinophysis acuminata and D. norvegica have mainly been abundant from March to December, whereas D. acuta has typically occurred in late summer and autumn (August-December). For all three species we have observed a narrowing of the peak season since 2002 at the same time as they have become less abundant. Coincident with these changes, the problem of the accumulation of DSP toxins in mussels along the southern coast of Norway has declined significantly, but it is still mainly restricted to the autumn. Why the cell concentration of Dinophysis spp. has declined after 2002 is not obvious, but this has occurred in a period with relatively high summer temperatures. The relatively simultaneous changes in physical, chemical and biological factors of the pelagic ecosystem along the southern coast of Norway indicate that complicated ecological interactions may be involved.

Human endonuclease III acts preferentially on DNA damage opposite guanine residues in DNA.

The human endonuclease III homologue (hNTH1) removes premutagenic cytosine damage from DNA. This includes 5-hydroxycytosine, which has increased potential for pairing with adenine, resulting in C --> T transition mutations. Here we report that hNTH1 acts on both 5-hydroxycytosine and abasic sites preferentially when these are situated opposite guanines in DNA. Discrimination against other opposite bases is strongly dependent on the presence of magnesium. To further elucidate this effect, we have introduced mutations in the helix-hairpin-helix domain of hNTH1 (K212S, P211R, +G212, and DeltaP211), and measured the kinetics of 5-hydroxycytosine removal of the mutants relative to wild type. The K212S and DeltaP211 (truncated hairpin) mutant proteins were both inactive, whereas the extended hairpin in the +G212 mutant diminished recognition and binding to 5-hydroxycytosine-containing DNA. The P211R mutant resembled native hNTH1, except for decreased specificity of binding. Despite the altered kinetic parameters, the active mutants retained the ability to discriminate against the pairing base, indicating that enzyme interactions with the opposite strand relies on other domains than the active site helix-hairpin-helix motif.