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The small, high-light-induced protein SliP4 is involved in the proper organization of photosynthetic complexes in thylakoid membranes of Synechocystis sp. PCC 6803

ABSTRACT: An increasing number of small proteins has been identified in the genomes of well-annotated model organisms including photosynthetic cyanobacteria such as Synechocystis sp. PCC 6803. A newly assigned protein comprising 37 amino acids was analyzed that is encoded upstream of the super-oxide dismutase SodB encoding gene. The initial hypothesis that this small protein might be functionally related to SodB could not be supported, instead we provide evidence that it fulfills important functions related to the organization of photosynthetic complexes. Therefore, we named it small light-induced protein of 4 kDa, SliP4. SliP4 is strongly induced under high-light-conditions and it is co-localized to photosystem I and II as well as NDH1 complexes on thylakoid membranes. Tagged SliP4 was used to purify NDH1 complexes, where it is especially associated with the subunits NdhF1 and NdhD1. Mutation of the protein-coding part in the sliP4 gene resulted in a high-light-sensitive phenotype, because the mutant was not further able to induce cyclic electron flow and state transitions under high-light conditions. Collectively our data indicate that SliP4 contributes to the association of NDH1 with the photosystem I and/or photosystem II complexes to facilitate different electron transfer modes under high light conditions.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Synechocystis Sp. Pcc 6803

SUBMITTER: Sandra Maass

LAB HEAD: Dörte Becher

PROVIDER: PXD036788 | Pride | 2023-06-07

REPOSITORIES: Pride

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Project description:The trophic condition related proteomes of an oxygenic photosynthetic cyanobacterium Synechocystis sp. PCC 6803 (glucose tolerant strain) were analyzed to get further insights into the metabolic traits governing the early exponential growth under photoautotrophic, mixotrophic and heterotrophic conditions. The cells were grown under constant light autotrophically (AT) in low (air-level) CO2 (ATLC) and in high CO2 (ATHC), mixotrophically (MT) in low (air-level) CO2 in the presence of glucose (MTLC) and heterotrophically in low (air-level) CO2 in the presence of glucose and only 10 min exposure to light every 24 hours (Light-Activated Heterotrophic Growth; LAHGLC). The proteomes of ATHC, MTLC and LAHGLC differed substantially from that of ATLC, particularly by downregulation of the inducible carbon concentrating mechanisms (CCM) and photorespiration related enzymes. On the contrary, under carbon-rich conditions (ATHC, MTLC, LAHGLC) the cells accumulated respiratory NAD(P)H dehydrogenase I complexes in the thylakoid membrane. In glucose supplemented cultures (MTLC, LAHGLC) a distinct NDH-2 protein, NdbA, additionally accumulated in the thylakoid membrane whilst the plasma membrane localized NdbC and ARTO decreased in abundance. The light-harvesting proteins together with the photosystem I and II subunits were uniquely depleted under LAHGLC condition, accumulated under ATHC and in MTLC remained at the level of the reference ATLC condition. The accumulation of P-transporters was unique, revealing only minor differences between ATLC and ATHC but strong up-regulation in MTLC and down-regulation in LAHGLC. This likely implies that MTLC stores energy surplus in the highly energetic bonds of polyphosphate polymer that can be used under unfavorable growth conditions. It is concluded that the rigor of cell growth in MTLC condition results to a great extent from high intracellular inorganic carbon conditions created upon glucose breakdown and release of CO2, beside the direct utilization of glucose-derived carbon skeletons for growth. This combination provides the MTLC cultures with excellent conditions for growth that often exceeds that of the mere photoautotrophic growth at high CO2.

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The small, high-light-induced protein SliP4 is involved in the proper organization of photosynthetic complexes in thylakoid membranes of Synechocystis sp. PCC 6803

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