Elucidating light-induced changes in excitation energy transfer of photosystem I and II in whole cells of two model cyanobacteria.

Excitation energy transfer between the photochemically active protein complexes is key for photosynthetic processes. Phototrophic organisms like cyanobacteria experience subtle changes in irradiance under natural conditions. Such changes need adjustments to the excitation energy transfer between the photosystems for sustainable growth.

Arg24 and 26 of the D2 protein are important for photosystem II assembly and plastoquinol exchange in Synechocystis sp. PCC 6803.

Photosystem II (PS II) assembly is a stepwise process involving preassembly complexes or modules focused around four core PS II proteins. The current model of PS II assembly in cyanobacteria is derived from studies involving the deletion of one or more of these core subunits. Such deletions may destabilize other PS II assembly intermediates, making constructing a clear picture of the intermediate events difficult.

A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria.

Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site.

Phylogenetic and spectroscopic insights on the evolution of core antenna proteins in cyanobacteria.

Light harvesting by antenna systems is the initial step in a series of electron-transfer reactions in all photosynthetic organisms, leading to energy trapping by reaction center proteins. Cyanobacteria are an ecologically diverse group and are the simplest organisms capable of oxygenic photosynthesis. The primary light-harvesting antenna in cyanobacteria is the large membrane extrinsic pigment-protein complex called the phycobilisome.

Energy dissipation efficiency in the CP43 assembly intermediate complex of photosystem II.

Photosystem II in oxygenic organisms is a large membrane bound rapidly turning over pigment protein complex. During its biogenesis, multiple assembly intermediates are formed, including the CP43-preassembly complex (pCP43). To understand the energy transfer dynamics in pCP43, we first engineered a His-tagged version of the CP43 in a CP47-less strain of the cyanobacterium Synechocystis 6803.

Photosynthetic modulation during the diurnal cycle in a unicellular diazotrophic cyanobacterium grown under nitrogen-replete and nitrogen-fixing conditions.

Cyanobacteria are the only oxygenic photosynthetic organisms that can fix nitrogen. In diazotrophic cyanobacteria, the regulation of photosynthesis during the diurnal cycle is hypothesized to be linked with nitrogen fixation and involve the D1 protein isoform PsbA4. The amount of bioavailable nitrogen has a major impact on productivity in aqueous environments.

Introduction of cysteine-mediated quenching in the CP43 protein of photosystem II builds resilience to high-light stress in a cyanobacterium.

Photosystem (PS) II is prone to photodamage both as a direct consequence of light, and indirectly by producing reactive oxygen species. Engineering high-light tolerance in cyanobacteria with minimal impact on PSII function is desirable in synthetic biology. IsiA, a CP43 homolog found exclusively in cyanobacteria, can dissipate excess light energy.

Psb27, a photosystem II assembly protein, enables quenching of excess light energy during its participation in the PSII lifecycle.

Photosystem II (PSII), the enzyme responsible for oxidizing water into molecular oxygen, undergoes a complex lifecycle during which multiple assembly proteins transiently bind to and depart from PSII assembly intermediate complexes. Psb27 is one such protein. It associates with the CP43 chlorophyll-binding subunit of PSII to form a Psb27-PSII sub-complex that constitutes 7-10% of the total PSII pool.

PsbX maintains efficient electron transport in Photosystem II and reduces susceptibility to high light in Synechocystis sp. PCC 6803.

PsbX is a 4.1 kDa intrinsic Photosystem II (PS II) protein, found together with the low-molecular-weight proteins, PsbY and PsbJ, in proximity to cytochrome b. The function of PsbX is not yet fully characterized but PsbX may play a role in the exchange of the secondary plastoquinone electron acceptor Q with the quinone pool in the thylakoid membrane.

A Novel Mode of Photoprotection Mediated by a Cysteine Residue in the Chlorophyll Protein IsiA.

Oxygenic photosynthetic organisms have evolved a multitude of mechanisms for protection against high-light stress. IsiA, a chlorophyll -binding cyanobacterial protein, serves as an accessory antenna complex for photosystem I. Intriguingly, IsiA can also function as an independent pigment protein complex in the thylakoid membrane and facilitate the dissipation of excess energy, providing photoprotection.

Stabilization of Photosystem II by the PsbT protein impacts photodamage, repair and biogenesis.

Photosystem II (PS II) catalyzes the light-driven process of water splitting in oxygenic photosynthesis. Four core membrane-spanning proteins, including D1 that binds the majority of the redox-active co-factors, are surrounded by 13 low-molecular-weight (LMW) proteins. We previously observed that deletion of the LMW PsbT protein in the cyanobacterium Synechocystis sp.

Tunable Repression of Key Photosynthetic Processes Using Cas12a CRISPR Interference in the Fast-Growing Cyanobacterium sp. UTEX 2973.

Cyanobacteria are photoautotrophic prokaryotes that serve as key model organisms to study basic photosynthetic processes and are potential carbon-negative production chassis for commodity and high-value chemicals. The development of new synthetic biology tools and improvement of current ones is a requisite for furthering these organisms as models and production vehicles. CRISPR interference (CRISPRi) allows for targeted gene repression using a DNase-dead Cas nuclease ("dCas").