Biology subjects

Raja, S. O.

Publications and source records attributed to Raja, S. O..

4 recordsLinked to original sources

bioRxiv2018

Euchromatic histone methyltransferases regulate peripheral heterochromatin tethering via histone and non-histone protein methylations

Euchromatic histone methyltransferases (EHMTs), members of the KMT1 family, methylate histone and non-histone proteins. Here we uncover a novel role for EHMTs in regulating heterochromatin anchorage to the nuclear periphery (NP) via non-histone (LaminB1) methylations. We show that EHMTs methylates and stabilizes LaminB1 (LMNB1), which associates with the H3K9me2-marked peripheral heterochromatin. Loss of LMNB1 methylation or EHMTs abrogates the heterochromatin anchorage from the NP. We further demonstrate that the loss of EHMTs induces many hallmarks of aging including global reduction of H3K27methyl marks along with altered nuclear-morphology. Consistent with this, we observed a gradual depletion of EHMTs, which correlates with loss of methylated LMNB1 and peripheral heterochromatin in aging human fibroblasts. Restoration of EHMT expression reverts peripheral heterochromatin defect in aged cells. Collectively our work elucidates a new mechanism by which EHMTs regulate heterochromatin domain organization and reveals their impact on fundamental changes associated with the intrinsic aging process.

genetics↗

bioRxiv2017

Antiferromagnetic switch in serum

1.Ferritin contains naturally occurring iron oxide nanoparticle surrounded by a structured spherical array of peptide residues that provides tremendous stability to this iron storage protein. We use synthetic citrate coated Super Paramagnetic Iron Oxide Nanoparticles (SPIONs) and static magnetic field in exploring the Ferritin induced magnetic environment of human serum samples with varying ferritin level collected from thalassemic patients. We report anti-ferromagnetic properties of serum in patients with iron overloading. Magnetic pulling by an external magnetic field showed a cusp-like behavior with increasing concentration of serum Ferritin measured by standard ELISA based kit. A reduction in the extent of pulling after a threshold concentration of Ferritin (1500 ng/ml) suggests a Ferritin dependent magnetic switching.Negative magnetization (anti-ferromagnetization) was confirmed by Vibrating Sample Magnetometric (VSM) analysis of SPION-serum mixture containing very high level of Ferritin. Such magnetic switching may have a possible role in iron homeostasis during overloading of Ferritin.\n\n3. AbbreviationsSPIONs: Super Paramagnetic Iron Oxide Nanoparticles, VSM: Vibrating Sample Magnetometry, SQUID: Super conducting Quantum Interference Device, PCS: Photon Correlation Spectroscopy

biophysics↗

bioRxiv2017

Switchable amplification of fluoresence from a photosynthetic microbe

One known attribute of the photosynthetic apparatus is photon capture and generation of metabolic energy. The thermodynamic implications of fluorescence, invariably associated with the photosynthetic components is however poorly understood. In this paper we report a density dependent amplification of such fluorescence which can be interpreted as a thermodynamic strategy of controlled energy release by the cell. We show in support of this hypothesis that prolonged photo-exitation of cell free extract of Rhodobacter capsulatus SB1003 at 395 nm, induces fluorescence emission amplifying with time as long as the fluorophore density is above a critical level. The fact that the amplification disappears at low temperature and at dilute condition, is in accordance with the thermodynamic interpretation that energy is released as per requirement. Live cell imaging is also validation of the phenomenon even at the cellular level. Single cells of Rhodobacter capsulatus SB1003 shows time dependent loss of fluorescence, the process being reversed for cellular clusters. To explain the mechanism of this bistable fluorescence (F) amplification, variation of the scale free kinetic constant k=1/F (dF/dt) is studied at varying temperatures in presence and absence of static magnetic field. The sign of k shifts from positive to negative if T is lowered or if the system is diluted. But at low T, k again switches from negative to positive value, if static magnetic field is applied. The chain of events can be explained by a simple model assuming excretion of a porphyrin by the microbe and possible photon dependent aggregation behavior of such porphyrin complex, differential temperature and magnetic field sensitivity of the monomeric or aggregated forms of porphyrin being reported earlier.

biophysics↗

bioRxiv2017

Bistability In Fluorescence From A Purple Non-Sulfur Bacteria

Bistable optical emission has been observed for photosynthetic purple non-sulfur bacteria Rhodobacter capsulatus SB1003. The microbes respond to UV excitation (at 395nm) in a bifurcating way one branch corresponding to increase and the other corresponding to diminishing fluorescent emission in the range 590-685nm.The switching between such bifurcating branches can be observed when parameters like concentration, temperature are varied or static magnetic field is applied. Thus switching from amplification to reduction occurs if fluorophore concentration lowered. Again if temperature is lowered a steady quenching (instead of amplification) of fluorescence is observed. However presence of magnetic field of the order of 0.5 T reverts this and once again the systems resumes its fluoresence amplifying state. We propose that aggregation of bacterial porphyrin and regulation of such aggregation by photon excitation may explain this bistablity. Possible ecological implication of the photosynthetic bistability is suggested.

systems biology↗