Biology subjects

Nguyen, P. D. N.

Publications and source records attributed to Nguyen, P. D. N..

3 recordsLinked to original sources

bioRxiv2025

Actin monomers influence the interaction between Xenopus cyclase-associated protein 1 and actin filaments

Cyclase-associated protein (CAP) binds to both actin monomers and filaments and regulates multiple aspects of the actin dynamics including polymerization and depolymerization. CAP has been isolated from multiple species as a stable equimolar complex with actin monomer. However, functional significance of the CAP-actin complex is unknown. We previously demonstrated that native Xenopus cyclase-associated protein 1 (XCAP1) forms a 4:4 complex with actin. Here, we characterized how actin-free XCAP1 and the XCAP1-actin complex interact with actin filaments using high-speed atomic force microscopy and found that XCAP1-bound actin monomers influence dwell time and positional preference of XCAP1 on actin filaments. Actin-free XCAP1 bound to actin filaments transiently with a dwell time of [~]0.2 seconds. The XCAP1-actin complex also bound to actin filaments transiently but with a 3-to 5-fold longer dwell time than actin-free XCAP1. Actin-free XCAP1 bound to both side and ends of actin filaments with moderate preference to ends. However, the XCAP1-actin complex bound preferentially to the side of actin filaments. These results indicate that binding of actin monomers to XCAP1 affects its binding modes to actin filaments, suggesting that this might be a novel mechanism to regulate the effects of CAP on actin filaments.

biochemistry↗

bioRxiv2025

Mycobacterial DNA-binding protein 1 (MDP1) induces RNA condensation as revealed by high-speed AFM

Mycobacterial DNA-binding protein 1 (MDP1) is a histone-like protein in Mycobacterium tuberculosis (Mtb) that contributes to genome organization and dormancy adaptation. MDP1 consists of a structured HU-like region (HUR), and a post-translational modifications (PTMs)-enriched intrinsically disordered region (IDR), that regulate its function. While its role in DNA condensation is well established, how MDP1 interacts with RNA remains unclear, despite growing recognition of transcriptional regulation during dormancy. Here, by using total RNA from E. coli as a model substrate, we investigated whether MDP1 induces RNA condensation. Our high-speed AFM and optical microscopy analysis shows that native MDP1 from Mtb, rich in PTMs, forms globular RNA condensates. In contrast, MDP1 expressed in E. coli, which lacks PTMs, induces chain-like RNA condensates. Domain-specific analysis revealed that the IDR, the synergy between the IDR and HUR, and PTMs are essential for MDP1-induced RNA condensation. These findings suggest that MDP1 mediates RNA organization during dormancy.

biophysics↗

bioRxiv2021

Unraveling the host-selective toxic interaction of cassiicolin with lipid membranes and its cytotoxicity

Cassiicolin (Cas), a toxin produced by Corynespora cassiicola, is responsible for corynespora leaf fall disease in rubber trees. Currently, the molecular mechanism of the cytotoxicity of Cas and its host selectivity have not been fully elucidated. Here, we analyzed the binding of Cas1 and Cas2 to membranes consisting of different plant lipids and their membrane-disruption activities. Using high-speed atomic force microscopy and confocal microscopy, we reveal that the binding and disruption activities of Cas1 and Cas2 on lipid membranes are strongly dependent on the specific plant lipids. The negative phospholipids, glycerolipids, and sterols are more susceptible to membrane damage caused by Cas1 and Cas2 than neutral phospholipids and betaine lipids. Cytotoxicity tests on rubber leaves of RRIV 1, RRIV 4, and PB 255 clones suggest that the toxins cause necrosis of rubber leaves, except for the strong resistance of PB 255 against Cas2. Cryo- SEM analyses of necrotic leaf tissues exposed to Cas1 confirm that cytoplasmic membranes are vulnerable to the toxin. Thus, the host selectivity of Cas toxin is attained by the lipid-dependent binding activity of Cas to the membrane, and the cytotoxicity of Cas arises from its ability to form biofilm-like structures and disrupt specific membranes. Graphic Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=116 SRC="FIGDIR/small/438527v2_ufig1.gif" ALT="Figure 1"> View larger version (42K): org.highwire.dtl.DTLVardef@17ef3f4org.highwire.dtl.DTLVardef@1c24d41org.highwire.dtl.DTLVardef@15e071aorg.highwire.dtl.DTLVardef@24740e_HPS_FORMAT_FIGEXP M_FIG C_FIG HighlightsO_LICas1 and Cas2 directly damage and cause necrosis in the leaves of specific rubber clones. C_LIO_LICas1 and Cas2 can form biofilm-like structures on specific lipid membranes (negative phospholipids, glycerolipids, and sterols). The biofilm-like formation of Cas toxin plays an important role in selective disruption on lipid membranes. C_LIO_LIVulnerability of the specific cytoplasmic membranes to the selective Cas toxin that is the most remarkable feature of cytotoxicity of Cas toxin on plant cells. C_LI

biochemistry↗