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Biology subjects

Jiang, H.-W.

Publications and source records attributed to Jiang, H.-W..

2 recordsLinked to original sources

Structure and evolution of Photosystem I in the early-branching cyanobacterium Anthocerotibacter panamensis

Thylakoid-free cyanobacteria are thought to preserve ancestral traits of early-evolving organisms capable of oxygenic photosynthesis. However, and until recently, photosynthesis studies in thylakoid-free cyanobacteria were only possible in the model strain Gloeobacter violaceus. Here, we report the isolation, biochemical characterization, cryo-EM structure, and phylogenetic analysis of photosystem I from a newly-discovered thylakoid-free cyanobacterium, Anthocerotibacter panamensis, a distant relative of the genus Gloeobacter. We find that A. panamensis photosystem I exhibits a distinct carotenoid composition and has one conserved low-energy chlorophyll site, which was lost in G. violaceus. These features explain the capacity of A. panamensis to grow under high light intensity, unlike other Gloeobacteria. Furthermore, we find that, while at the sequence level photosystem I in thylakoid-free cyanobacteria has changed to a degree comparable to that of other strains, its subunit composition and oligomeric form might be identical to that of the most recent common ancestor of cyanobacteria.

plant biology↗

Specific Pupylation as IDEntity Reporter (SPIDER) for the identification of Protein-Biomolecule interactions

Protein-biomolecule interactions play pivotal roles in almost all biological processes, the identification of the interacting protein is essential. By combining a substrate-based proximity labelling activity from the pupylation pathway of Mycobacterium tuberculosis, and the streptavidin (SA)-biotin system, we developed Specific Pupylation as IDEntity Reporter (SPIDER) for identifying protein-biomolecular interactions. As a proof of principle, SPIDER was successfully applied for global identification of interacting proteins, including substrates for enzyme (CobB), the readers of m6A, the protein interactome of mRNA, and the target proteins of drug (lenalidomide). In addition, by SPIDER, we identified SARS-CoV-2 Omicron variant specific receptors on cell membrane and performed in-depth analysis for one candidate, Protein-g. These potential receptors could explain the differences between the Omicron variant and the Prototype strain, and further serve as target for combating the Omicron variant. Overall, we provide a robust technology which is applicable for a wide-range of protein-biomolecular interaction studies.

systems biology↗