Publications by authors named "M Dolores Ludevid"
Article Synopsis
- Optical trapping can reveal details about the structural and kinetic properties of cell components but is challenging due to the small difference in refractive indices between target structures and cytoplasm.
- Researchers propose creating spherical organelles within the endoplasmic reticulum, filled with specially designed proteins, to serve as better targets for optical trapping.
- These engineered organelles have a high refractive index and larger size, making them easier to manipulate with optical trapping techniques compared to traditional probes like subcellular organelles or synthetic beads.
Late Embryogenesis Abundant (LEA) proteins participate in plant stress responses and contribute to the acquisition of desiccation tolerance. In this report Rab28 LEA gene has been over-expressed in maize plants under a constitutive maize promoter. The expression of Rab28 transcripts led to the accumulation and stability of Rab28 protein in the transgenic plants.
View Article and Find Full Text PDFBackground: The N-terminal proline-rich domain (Zera) of the maize storage protein γ-zein, is able to induce the formation of endoplasmic reticulum (ER)-derived protein bodies (PBs) when fused to proteins of interest. This encapsulation enables a recombinant fused protein to escape from degradation and facilitates its recovery from plant biomass by gradient purification. The aim of the present work was to evaluate if induced PBs encapsulate additional proteins jointly with the recombinant protein.
View Article and Find Full Text PDFBackground: Xylanases deserve particular attention due to their potential application in the feed, pulp bleaching and paper industries. We have developed here an efficient system for the production of an active xylanase in tobacco plants fused to a proline-rich domain (Zera) of the maize storage protein γ-zein. Zera is a self-assembling domain able to form protein aggregates in vivo packed in newly formed endoplasmic reticulum-derived organelles known as protein bodies (PBs).
View Article and Find Full Text PDFArticle Synopsis
- The N-terminal proline-rich domain of γ-zein (Zera) is crucial for forming protein bodies (PBs) in maize and other eukaryotic cells, but specific sequence elements that aid in this process have not been fully identified.
- Research involved analyzing amino acid motifs in Zera to understand how it forms PB-like structures in Nicotiana benthamiana leaves, revealing that certain sequences influence Zera’s ability to oligomerize.
- Key findings indicate that while the (PPPVHL)(8) repeat region is most effective for Zera assembly, shorter repeats can also form small clusters, and two cysteine residues are essential for this process, leading to a