Author Correction: Widespread ground motion distribution caused by rupture directivity during the 2015 Gorkha, Nepal earthquake.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Widespread ground motion distribution caused by rupture directivity during the 2015 Gorkha, Nepal earthquake.

The ground motion and damage caused by the 2015 Gorkha, Nepal earthquake can be characterized by their widespread distributions to the east. Evidence from strong ground motions, regional acceleration duration, and teleseismic waveforms indicate that rupture directivity contributed significantly to these distributions. This phenomenon has been thought to occur only if a strike-slip or dip-slip rupture propagates to a site in the along-strike or updip direction, respectively. However, even though the earthquake was a dip-slip faulting event and its source fault strike was nearly eastward, evidence for rupture directivity is found in the eastward direction. Here, we explore the reasons for this apparent inconsistency by performing a joint source inversion of seismic and geodetic datasets, and conducting ground motion simulations. The results indicate that the earthquake occurred on the underthrusting Indian lithosphere, with a low dip angle, and that the fault rupture propagated in the along-strike direction at a velocity just slightly below the S-wave velocity. This low dip angle and fast rupture velocity produced rupture directivity in the along-strike direction, which caused widespread ground motion distribution and significant damage extending far eastwards, from central Nepal to Mount Everest.

Molecular characterization of organelle-type Nudix hydrolases in Arabidopsis.

Nudix (for nucleoside diphosphates linked to some moiety X) hydrolases act to hydrolyze ribonucleoside and deoxyribonucleoside triphosphates, nucleotide sugars, coenzymes, or dinucleoside polyphosphates. Arabidopsis (Arabidopsis thaliana) contains 27 genes encoding Nudix hydrolase homologues (AtNUDX1 to -27) with a predicted distribution in the cytosol, mitochondria, and chloroplasts. Previously, cytosolic Nudix hydrolases (AtNUDX1 to -11 and -25) were characterized. Here, we conducted a characterization of organelle-type AtNUDX proteins (AtNUDX12 to -24, -26, and -27). AtNUDX14 showed pyrophosphohydrolase activity toward both ADP-ribose and ADP-glucose, although its K(m) value was approximately 100-fold lower for ADP-ribose (13.0+/-0.7 microm) than for ADP-glucose (1,235+/-65 microm). AtNUDX15 hydrolyzed not only reduced coenzyme A (118.7+/-3.4 microm) but also a wide range of its derivatives. AtNUDX19 showed pyrophosphohydrolase activity toward both NADH (335.3+/-5.4 microm) and NADPH (36.9+/-3.5 microm). AtNUDX23 had flavin adenine dinucleotide pyrophosphohydrolase activity (9.1+/-0.9 microm). Both AtNUDX26 and AtNUDX27 hydrolyzed diadenosine polyphosphates (n=4-5). A confocal microscopic analysis using a green fluorescent protein fusion protein showed that AtNUDX15 is distributed in mitochondria and AtNUDX14 -19, -23, -26, and -27 are distributed in chloroplasts. These AtNUDX mRNAs were detected ubiquitously in various Arabidopsis tissues. The T-DNA insertion mutants of AtNUDX13, -14, -15, -19, -20, -21, -25, -26, and -27 did not exhibit any phenotypical differences under normal growth conditions. These results suggest that Nudix hydrolases in Arabidopsis control a variety of metabolites and are pertinent to a wide range of physiological processes.