384 research outputs found

    Soil organic carbon stock in natural and restored mangrove forests in Pichavaram south-east coast of India

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    801-808Mangrove ecosystem is one of the important coastal ecosystems providing ecological security of the coastal area and livelihood security to the coastal fishermen.  Besides it plays an important role in carbon sequestration as large amount of carbon is stored in the below ground biomass. The role of mangrove restoration in carbon stocking has not been studied comprehensively either globally or nationally. The aim of the present study is to quantify the soil organic carbon stock and carbon sequestration rate of the different age groups of restored and natural stands of Pichavaram mangroves forest. The soil organic carbon stock of the upper soil layer (0–90 cm) of six different sites from natural mangrove stands, 21years, 17 years, 16 years, 15 years and 12 years old stands were 146.1(Mg C ha-1), 99.29 (Mg C ha-1), 93.18 (Mg C ha-1), 57.41 (Mg C ha-1), 95.54 (Mg C ha-1) and 84.84 (Mg C ha-1), respectively. Carbon sequestration rate of Pichavaram mangrove forests ranged from 2.33 to 4.44 g C m-2 year-1. The result of the study reveals that soil organic carbon stock and burial rate were high in natural mangrove area than the restored areas. In this regard, restoration and rehabilitation of mangroves is required for preserving the ecologically important mangroves ecosystem to mitigate the impacts of climate change

    Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis

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    The PARK2 gene is mutated in 50% of autosomal recessive juvenile parkinsonism (ARJP) cases. It encodes parkin, an E3 ubiquitin ligase of the RBR family. Parkin exists in an autoinhibited state that is activated by phosphorylation of its N‐terminal ubiquitin‐like (Ubl) domain and binding of phosphoubiquitin. We describe the 1.8 Å crystal structure of human parkin in its fully inhibited state and identify the key interfaces to maintain parkin inhibition. We identify the phosphoubiquitin‐binding interface, provide a model for the phosphoubiquitin–parkin complex and show how phosphorylation of the Ubl domain primes parkin for optimal phosphoubiquitin binding. Furthermore, we demonstrate that the addition of phosphoubiquitin leads to displacement of the Ubl domain through loss of structure, unveiling a ubiquitin‐binding site used by the E2~Ub conjugate, thus leading to active parkin. We find the role of the Ubl domain is to prevent parkin activity in the absence of the phosphorylation signals, and propose a model for parkin inhibition, optimization for phosphoubiquitin recruitment, release of inhibition by the Ubl domain and engagement with an E2~Ub conjugate. Taken together, this model provides a mechanistic framework for activating parkin
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