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Rodriguez, J.

Publications and source records attributed to Rodriguez, J..

4 recordsLinked to original sources

Pollinator size and its consequences: Predictive allometry for pollinating insects

O_LIBody size is an integral functional trait that underlies pollination-related ecological processes, yet it is often impractical to measure directly. Allometric scaling laws have been used to overcome this problem. However, most existing models rely upon small sample sizes, geographically restricted sampling and have limited applicability for non-bee taxa. Predictive allometric models that consider biogeography, phylogenetic relatedness and intraspecific variation are urgently required to ensure greater accuracy.\nC_LIO_LIHere, we measured body size, as dry weight, and intertegular distance (ITD) of 391 bee species (4035 specimens) and 103 hoverfly species (399 specimens) across four biogeographic regions: Australia, Europe, North America and South America. We updated existing models within a Bayesian mixed-model framework to test the power of ITD to predict interspecific variation in pollinator dry weight in interaction with different co-variates: phylogeny or taxonomy, sexual dimorphism and biogeographic region. In addition, we used ordinary least squares (OLS) regression to assess intraspecific dry weight - ITD relationships for 10 bee and five hoverfly species.\nC_LIO_LIIncluding co-variates led to more robust interspecific body size predictions for both bees (Bayesian R2: 0.946; {Delta}R2 0.047) and hoverflies (Bayesian R2: 0.821; {Delta}R2 0.058) relative to models with ITD alone. In contrast, at the intraspecific level, our results demonstrate that ITD is an inconsistent predictor of body size for bees (R2: 0.02 - 0.66) and hoverflies (R2: -0.11 - 0.44).\nC_LIO_LITherefore, predictive allometry is more suitable for interspecific comparative analyses than assessing intraspecific variation. Collectively, these models form the basis of the dynamic R package, pollimetry, which provides a comprehensive resource for allometric research concerning insect pollinators worldwide.\nC_LI

ecology

PI31 is an adaptor protein for proteasome transport in axons

Protein degradation by the ubiquitin-proteasome system (UPS) is critical for neuronal development, plasticity and function. Neurons utilize microtubule-dependent molecular motors to allocate proteasomes to synapses, but how proteasomes are coupled to motor proteins and how this transport is regulated to meet changing demand for protein breakdown remains largely unknown. We show that the conserved proteasome-binding protein PI31 serves as an adaptor to directly couple proteasomes with dynein light chain proteins (DYNLL1/2). Inactivation of PI31 inhibits proteasome motility in axons and disrupts synaptic protein homeostasis, structure and function. Moreover, phosphorylation of PI31 at a conserved site by p38 MAP kinase promotes binding to DYNLL1/2, and a non-phosphorable PI31 mutant impairs proteasome movement in axons, suggesting a mechanism to regulate loading of proteasomes onto motor proteins. Because mutations affecting PI31 activity are associated with human neurodegenerative diseases, impairment of PI31-mediated axonal transport of proteasomes may be the root cause of these disorders.

cell biology

Analysis of global and site-specific radiation damage in cryo-EM

Micro-crystal electron diffraction (MicroED) is an emerging method in cryo-EM for structure determination using nanocrystals. It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data.

biochemistry

MicroED Structures from Micrometer Thick Protein Crystals

Theoretical calculations suggest that crystals exceeding 100 nm thickness are excluded by dynamical scattering from successful structure determination using microcrystal electron diffraction (MicroED). These calculations are at odds with experimental results where MicroED structures have been determined from significantly thicker crystals. Here we systematically evaluate the influence of thickness on the accuracy of MicroED intensities and the ability to determine structures from protein crystals one micrometer thick. To do so, we compare ab initio structures of a human prion protein segment determined from thin crystals to those determined from crystals up to one micrometer thick. We also compare molecular replacement solutions from crystals of varying thickness for a larger globular protein, proteinase K. Our results indicate that structures can be reliably determined from crystals at least an order of magnitude thicker than previously suggested by simulation, opening the possibility for an even broader range of MicroED experiments.\n\nSummaryAtomic resolution protein structures can be determined by MicroED from crystals that surpass the theoretical maximum thickness limit by an order of magnitude.

biochemistry