The May 29 2008 earthquake aftershock sequence within the South Iceland Seismic Zone: Fault locations and source parameters of aftershocks

The mid-Atlantic plate boundary breaks up into a series of segments across Iceland. The South Iceland Seismic Zone (SISZ) is a complex transform zone where left-lateral E-W shear between the Reykjanes Peninsula Rift Zone and the Eastern Volcanic Zone is accommodated by bookshelf faulting along N-S lateral strike-slip faults. The SISZ is also a transient feature, migrating sideways in response to the southward propagation of the Eastern Volcanic Zone. Sequences of large earthquakes (M > 6) lasting from days to years and affecting most of the seismic zone have occurred repeatedly in historical time (last 1100 years), separated by intervals of relative quiescence lasting decades to more than a century. On May 29 2008, a Mw 6.1 earthquake struck the western part of the South Iceland Seismic Zone, followed within seconds by a slightly smaller event on a second fault ~5 km further west. Aftershocks, detected by a temporal array of 11 seismometers and three permanent Icelandic Meteorological Office stations were located using an automated Coalescence Microseismic Mapping technique. The epicenters delineate two major and several smaller N-S faults as well as an E-W zone of activity stretching further west into the Reykjanes Peninsula Rift Zone. Fault plane solutions show both right lateral and oblique strike slip mechanisms along the two major N-S faults. The aftershocks deepen from 3-5 km in the north to 8-9 km in the south, suggesting that the main faults dip southwards. The faulting is interpreted to be driven by the local stress due to transform motion between two parallel segments of the divergent plate boundary crossing Iceland

Deletion of a cytotoxic, N-terminal putative signal peptide results in a significant increase in production yields in Escherichia coli and improved specific activity of Cel12A from Rhodothermus marinus

The thermostable cellulase Cel12A from Rhodothermus marinus was produced at extremely low levels when expressed in Escherichia coli and was cytotoxic to the cells. In addition, severe aggregation occurred when moderately high concentrations of the enzyme were heat-treated at 65°C, the growth optimum of R. marinus. Sequence analysis revealed that the catalytic module of this enzyme is preceded by a typical linker sequence and a highly hydrophobic putative signal peptide. Two deletion mutants lacking this hydrophobic region were cloned and successfully expressed in E. coli. These results indicated that the N-terminal putative signal peptide was responsible for the toxicity of the full-length enzyme in the host organism. This was further corroborated by cloning and expressing the hydrophobic N-terminal domain in E. coli, which resulted in extensive cell lysis. The deletion mutants, made up of either the catalytic module of Cel12A or the catalytic module and the putative linker sequence, were characterised and their properties compared to those of the full-length enzyme. The specific activity of the mutants was approximately threefold higher than that of the full-length enzyme. Both mutant proteins were highly thermostable, with half-lives exceeding 2 h at 90°C and unfolding temperatures up to 103°C