Subsurface signatures and timing of extreme wave events along the Southeast Indian coast

Written history's limitation becomes apparent when attempting to document the predecessors of extreme coastal events in the Indian Ocean, from 550-700 years in Thailand and 1000 years in Indonesia. Detailed ground-penetrating radar (GPR) surveys in Mahabalipuram, southeast India, complemented with sedimentological analyses, magnetic susceptibility measurements, and optical dating provide strong evidence of extreme wave events during the past 3700 years. The diagnostic event signatures include the extent and elevation of the deposits, as well as morphologic similarity of buried erosional scarps to those reported in northern Sumatra region. Optical ages immediately overlying the imaged discontinuities that coincides with high concentration of heavy minerals date the erosional events to 340 ± 35, 350 ± 20, 490 ± 30, 880 ± 40, 1080 ± 60, 1175 ± 188, 2193 ± 266, 2235 ± 881, 2489 ± 293, 2450 ± 130, 2585 ± 609, 3710 ± 200 years ago. These evidences are crucial in reconstructing paleo extreme wave events and will pave the way for regional correlation of erosional horizons along the northern margin of Indian Ocean

Deamination of 6-Aminodeoxyfutalosine in Menaquinone Biosynthesis by Distantly Related Enzymes

Proteins of unknown function belonging to cog1816 and cog0402 were characterized. Sav2595 from Steptomyces avermitilis MA-4680, Acel0264 from Acidothermus cellulolyticus 11B, Nis0429 from Nitratiruptor sp. SB155-2 and Dr0824 from Deinococcus radiodurans R1 were cloned, purified, and their substrate profiles determined. These enzymes were previously incorrectly annotated as adenosine deaminases or chlorohydrolases. It was shown here that these enzymes actually deaminate 6-aminodeoxyfutalosine. The deamination of 6-aminodeoxyfutalosine is part of an alternative menaquinone biosynthetic pathway that involves the formation of futalosine. 6-Aminodeoxyfutalosine is deaminated by these enzymes with catalytic efficiencies greater than 10(5) M(−1) s(−1), K(m) values of 0.9 to 6.0 μM and k(cat) values of 1.2 to 8.6 s(−1). Adenosine, 2′-deoxyadenosine, thiomethyladenosine, and S-adenosylhomocysteine are deaminated at least an order of magnitude slower than 6-aminodeoxyfutalosine. The crystal structure of Nis0429 was determined and the substrate, 6-aminodeoxyfutalosine, was positioned in the active site, based on the presence of adventitiously bound benzoic acid. In this model Ser-145 interacts with the carboxylate moiety of the substrate. The structure of Dr0824 was also determined, but a collapsed active site pocket prevented docking of substrates. A computational model of Sav2595 was built based on the crystal structure of adenosine deaminase and substrates were docked. The model predicted a conserved arginine after β-strand 1 to be partially responsible for the substrate specificity of Sav2595

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