{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-2.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-1.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-1.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-2.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B2.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-1-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-1-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-1-1.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-2.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-1.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-1.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-2.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B2.mzid"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B1-1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B4-1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072813/B2.mgf"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"submitter":["Kuo-En Chen"],"software":[""],"tissue":["Whole Body"],"sample_protocol":["The chlorophyll a content of the purified fraction was determined by the method described by McKinney (1941)56. The gradient gels used for HrCN-PAGE, SDS-PAGE, and 2D-PAGE were poured in-house as per the protocol described earlier32,55.  For immunoblot analysis (Figure S2A, B), the proteins (refer Figure S2A-B legend for sample details) were separated on a denaturing gel (refer Figure S2A-B for details) and transferred to a PVDF membrane. The membranes were probed with either anti-IsiA antibody (Catalog number- AS06 111, Agrisera AB, Sweden) or anti-6×his antibody (Catalog number- PA1-983B, Invitrogen, USA) at dilutions of 1:1000 and 1:3000, respectively. The blots were visualized by probing with anti-rabbit-HRP conjugate secondary antibody (catalog number- A0545, Sigma-Aldrich, USA) using enhanced chemiluminescence. The purified IsiA2-containing complexes were separated on a 4-16% in-house poured native gel; the green bands, B1-3, were excised and analyzed by spectroscopy and mass spectrometry. The western blots and clear native gels were visualized by using either chemiluminescence or the 700 nm channel, respectively, of the LI-COR Odyssey® XF imaging system.  Protein complexes separated by native gel electrophoresis were subjected to in-gel digestion for subsequent mass spectrometry analysis. Individual protein bands were excised using a clean scalpel blade and cut into approximately 1 mm³ pieces, which were then transferred to clean 1.5 mL Eppendorf tubes. Gel pieces were destained with 250 μL of destaining buffer (25% acetonitrile (ACN) in 25 mM ammonium bicarbonate (ABC)). The buffer was replaced every 10 minutes until the gel pieces were completely colorless. Following destaining, gel pieces were reduced with 200 mM DTT in 25 mM ABC buffer for 1 hour at room temperature, followed by alkylation with 200 mM iodoacetamide (IAM) in 25 mM ABC buffer for 1 hour in the dark. The gel pieces were then washed with 200 μL of 25% ACN/25 mM ABC buffer for 5 minutes, followed by dehydration with 100 μL of 100% ACN for 5 minutes until the gel pieces turned completely white. After removing ACN, the gel pieces were dried completely using a SpeedVac concentrator. The dried gel pieces were rehydrated with 150 μL of 25 mM ABC buffer containing 1 μg of sequencing-grade modified trypsin (Promega) and incubated at 37 °C for 16 hours. Following digestion, peptides were extracted by adding 50 μL of 50% ACN/5% trifluoroacetic acid (TFA) and sonicating in an ultrasonic water bath (10 seconds on, 10 seconds off, repeated 10 times). After centrifugation, the supernatant was collected into a new 1.5 mL Eppendorf tube. A second extraction was performed by adding 150 μL of 50% ACN/5% TFA to the gel pieces, and the supernatant was combined with the first extract. The pooled extracts were dried using a SpeedVac concentrator, reconstituted in 100 μL of 0.1% TFA, and desalted using Pierce™ C18 Tips (Thermo Scientific). Peptides were eluted in 50 µL of 75% acetonitrile and 0.1% acetic acid, lyophilized again, and resuspended in 15 µL of 5% acetonitrile and 0.1% formic acid for LC-MS/MS analysis. Nano-scale liquid chromatography separation of the tryptic peptides was performed using a Dionex Ultimate 3000 Rapid Separation system equipped with a 75 µm × 25 cm Acclaim PepMap RSLC C18 column (Thermo Fisher Scientific), in combination with a 2 hr linear 4–24% ACN gradient in 0.1% formic acid and a flow rate of 250 nL/min. Eluted peptides were analyzed online by a Q-Exactive Plus spectrometer (Thermo Fisher Scientific) in the positive electrospray ionization (ESI) mode. Full MS scans were performed in a mass range of 380–1600 m/z at a resolution of 70,000, with an automatic gain control (AGC) target of 3 × 106 and a maximum injection time of 200 ms. Data-dependent acquisition (DDA) was applied to fragment the top fifteen most intense peaks using high-energy collision-induced dissociation (HCD) at a normalized collision energy of 28. An intensity threshold of 4 × 104 counts and an isolation window of 3.0 m/z were applied. Precursor ions with unassigned charges or charges of +1 to +8 or > +8 were excluded. MS/MS scans were collected at a resolution of 17,500, with an AGC target of 2 × 105 and a maximum fill time of 300 ms. Dynamic exclusion was performed with a repeat count of 2 and an exclusion duration of 30 s, while the minimum MS ion count for triggering tandem MS was set to 4 × 103 counts."],"repository":["Pride"],"labhead":["Kuo-En Chen"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Department of Biology, Washington University in St. Louis"],"publication":["Not available"],"submitter_affiliation":["Department of Biology, Washington University in St. Louis"],"labhead_mail":["kuo-en@wustl.edu"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Disease Free"],"submitter_keywords":["Isia","Spectroscopy","Time-resolved fluorescence","Light harvesting","Anabaena sp. pcc 7120","Energy transfer","Antenna proteins","Iron-stress"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072813"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry raw data were processed using Proteome Discoverer 2.5 (Thermo Fisher Scientific) for peptide identification and protein abundance calculation. Protein abundances were subsequently normalized against trypsin, which was spiked into each sample at equal amounts during sample preparation as an internal standard. Trypsin abundance showed excellent consistency across samples (CV = 3.33%), confirming minimal technical variation and validating the normalization approach. To ensure high-confidence protein identification, stringent filtering criteria were applied: proteins identified by at least two peptides, including a minimum of one unique peptide, were selected for downstream analysis and data visualization."],"omics_type":["Proteomics"],"species":["Nostoc Sp. Pcc 7120 = Fachb-418"],"submitter_mail":["kuo-en@wustl.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD072813"],"additional_accession":[]},"is_claimable":false,"name":"Photosystem I Structural Fusion with IsiA Enhances Light-Harvesting Capabilities of Filamentous Cyanobacterium During Iron Deficiency","description":"Iron deficiency impairs energy capture and photosynthetic electron transport, leading to remodeling of photosynthetic complexes, mainly impacting photosystem I. In Anabaena sp. PCC 7120, this remodeling includes a change in the oligomeric state of PSI and the formation of a unique antenna system with covalently attached IsiA2-PSI complex, along with other IsiA homologs. This study describes the spectroscopic properties of three types of IsiA2-containing complexes and details their energy-transfer efficiency. Based on spectral data and Mass-Spec analysis of these complexes, a proposed model suggests that antenna modulation, influenced by the intracellular redox state, could regulate PSI activity during iron 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