Biology subjects

kammara, R.

Publications and source records attributed to kammara, R..

2 recordsLinked to original sources

bioRxiv2023

Sapodilla rTLP exists as a monomer, dimer with β-1, 3-glucanase and antifungal activity.

The present study deals in understanding the structure-function relationship of Sapodilla thaumatin-like protein (TLP). Most of the TLPs known to be stimulated in response to biotic, and abiotic stress. Few TLPs possess both antifungal and enzymatic properties, only very few TLPs possess either of the activity or none of the attributes. This characteristic of TLPs offer great challenges to examine its functional differences among its members, though they are structurally homologous. Therefore, we were concerned to see the functionality of Sapodilla TLP, by cloning in E. coli, expression, purification, and characterization. Being a plant derived protein, it possesses post-translational modifications such as the presence of disulfide bonds. Hence, we proposed to adapt various protein purification tools to purify and to obtain biologically active protein. The refolded and purified rTLP (recombinant TLP) exists as a monomer and dimer with {beta}-1, 3-glucanase, and antifungal activity. The structure, function, relationship studies of rTLP (through deletion and site directed mutagenesis), observed to knock out the dimeric nature. Lastly, structural bioinformatics of rTLP reveal that their primary structural types are - {beta}- and non-helical structures.

plant biology↗

bioRxiv2022

Understanding the necessity of regulatory protein machinery in heterologous expression of class-III type of Ocins.

To date, there have been no or just a few reports of successful cloning and expression to create biologically active ocins or bacteriocins. Cloning, expression, and production of class I ocins are problematic because of their structural arrangements, coordinated functions, size, and posttranslational modifications. In the case of class III ocins, there are no reports of obtaining biological active proteins to date. Because of their growing importance, use and rapid functions require understanding mechanistic aspects to obtain biological active protein. As a result, we intend to clone and express the class III type. Also, by fusion or chimaera, they reshape class I types that lack posttranslational modifications into class III. Therefore, this construct resembles a class III type ocin. With the exception of Zoocin, expression of the proteins was found to be physiologically ineffective after cloning. But, few cell morphological changes such as elongation, aggregation, and the formation of terminal hyphae were observed. However, it was discovered that the target indicator had been altered to Vibrio spp. in a few. Finally, we confirm the existence of unidentified additional intrinsic factors for succesful expression to obtain biologically active protein.

microbiology↗