Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.

Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or \u27procapsid\u27) built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion. Here, we provide structural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinity binding to the large terminase packaging protein, and a symmetric ring in the mature virion (MV-portal) that has negligible affinity for the packaging motor. Modelling studies indicate the structure of PC-portal is incompatible with DNA coaxially spooled around the portal vertex, suggesting that newly packaged DNA triggers the switch from PC- to MV-conformation. Thus, we propose the signal for termination of \u27Headful Packaging\u27 is a DNA-dependent symmetrization of portal protein

Oligomerization, Conformational Stability and Thermal Unfolding of Harpin, HrpZPss and Its Hypersensitive Response-Inducing C-Terminal Fragment, C-214-HrpZPss.

HrpZ-a harpin from Pseudomonas syringae-is a highly thermostable protein that exhibits multifunctional abilities e.g., it elicits hypersensitive response (HR), enhances plant growth, acts as a virulence factor, and forms pores in plant plasma membranes as well as artificial membranes. However, the molecular mechanism of its biological activity and high thermal stability remained poorly understood. HR inducing abilities of non-overlapping short deletion mutants of harpins put further constraints on the ability to establish structure-activity relationships. We characterized HrpZPss from Pseudomonas syringae pv. syringae and its HR inducing C-terminal fragment with 214 amino acids (C-214-HrpZPss) using calorimetric, spectroscopic and microscopic approaches. Both C-214-HrpZPss and HrpZPss were found to form oligomers. We propose that leucine-zipper-like motifs may take part in the formation of oligomeric aggregates, and oligomerization could be related to HR elicitation. CD, DSC and fluorescence studies showed that the thermal unfolding of these proteins is complex and involves multiple steps. The comparable conformational stability at 25°C (∼10.0 kcal/mol) of HrpZPss and C-214-HrpZPss further suggest that their structures are flexible, and the flexibility allows them to adopt proper conformation for multifunctional abilities

Differential recognition of canonical NF-κB dimers by Importin α3

Nuclear translocation of the p50/p65 heterodimer is essential for NF-κB signaling. In unstimulated cells, p50/p65 is retained by the inhibitor IκBα in the cytoplasm that masks the p65-nuclear localization sequence (NLS). Upon activation, p50/p65 is translocated into the nucleus by the adapter importin α3 and the receptor importin β. Here, we describe a bipartite NLS in p50/p65, analogous to nucleoplasmin NLS but exposed in trans. Importin α3 accommodates the p50- and p65-NLSs at the major and minor NLS-binding pockets, respectively. The p50-NLS is the predominant binding determinant, while the p65-NLS induces a conformational change in the Armadillo 7 of importin α3 that stabilizes a helical conformation of the p65-NLS. Neither conformational change was observed for importin α1, which makes fewer bonds with the p50/p65 NLSs, explaining the preference for α3. We propose that importin α3 discriminates between the transcriptionally active p50/p65 heterodimer and p50/p50 and p65/65 homodimers, ensuring fidelity in NF-κB signaling

Wildlife Santuaries of Rajasthan

Volume: 61Start Page: 27End Page: 3

Farmers' Knowledge on Feeding Practices of Dairy Animals in Jhansi District

ABSTRAC

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Not AvailableCollective action approaches plays a significant role in solving marketing problems like providingthe remunerative price of the product, eliminates the intermediaries from the agriculture valuechain, and enhance the direct marketing between farmers and consumers. In these references, anew collective action approach being popularised in India i.e., farmer producer company. So, it isimportant to study the socio-economic characteristics of dairy farmers, motivational factors, and thereasons behind joining the FPCs. Hence a study was conducted from January 2020 at the threestates i.e. Rajasthan, Uttar Pradesh, and Madhya Pradesh of India to investigate the socio-economic profile, motivational factors, and the reasons behind joining the FPCs among farmers.Primary data was collected through a semi-structured interview schedule using a sample of 360farmers selected from twelve dairy-based FPCs of three states. Data were analyzed throughfrequency, range, and percentage. It was found that most farmers were middle-aged, possesssmall landholding, educated up to graduate level. The most important reason behind taking the membership of FPCs was to enhance the family income through FPCs, better price realization byFPCs, and quick payment settlement. Due to the above reasons, most of the farmers want to joinFPCs in study areas. The result of the present study helps to enhance the membership of farmerProducer Company through formulating a suitable strategy that should attract the farmer to joiningthe farmer producer company. This also helps to identify the motivation sources and their credibilityamong farmers for convincing them for joining FPCs. It was also found that the participation offarmers in dairy-based farmer producer companies is largely dependent on the socio-economic characteristics of the dairy farmers.Not Availabl