{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-CikB-APEX2__IPTG_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-ManS-APEX2__IPTG_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-RpaA-APEX2__IPTG_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS__IPTG_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-CikB-APEX2__IPTG_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-NblS-APEX2__IPTG_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-NblS-APEX2__IPTG_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS__IPTG_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-ManS-APEX2__IPTG_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-RpaA-APEX2__IPTG_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-NblS-APEX2__IPTG_rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS__IPTG_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-ManS-APEX2__IPTG_rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-CikB-APEX2__IPTG_rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-RpaA-APEX2__IPTG_rep2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/UP000002717_1140.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-CikB-APEX2_vs_CscB-SPS.rar.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-NblS-APEX2_vs_CscB-SPS_search.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-NblS-APEX2_vs_CscB-SPS.rar.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-ManS-APEX2_vs_CscB-SPS.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-RpaA-APEX2_vs_CscB-SPS.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-ManS-APEX2_vs_CscB-SPS_search.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-CikB-APEX2_vs_CscB-SPS_search.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD036717/CscB-SPS-RpaA-APEX2_vs_CscB-SPS_search.rar"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["ducatdan@msu.edu"],"submitter":["María Santos-Merino"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":[""],"submitter_keywords":["Two-component system","Sucrose","Cyanobacteria","Source-sink balance"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD036717"],"tissue":["Photosynthetic Cell"],"sample_protocol":["50 mL cultures of S. elongatus PCC 7942 strains were pelleted by centrifugation at 4,500 x g for 30 min at 4 °C. Cells were resuspended in 4 mL BG11 medium with 2.5 mM biotin phenol and transferred to a six-well plate. Six-well plates were incubated for 30 min in the growing conditions of S. elongatus cultures. Samples were then pelleted by centrifugation (2 min at 12,000 x g) in a 2 mL tube and resuspended in 1 mL PBS pH 7.8. 10 µL of 100 mM H2O2 was added and cells were inverted for 30 s before pelleting for 30 s at 12,000 x g. Cells were resuspended three times in quencher solution (PBS with 10 mM sodium ascorbate, 5 mM Trolox and 10 mM sodium azide) and pelleted. The supernatant was removed, and the cell pellets were frozen at −80 °C for storage and to facilitate cell lysis. Total protein was extracted by bead-beating in 150 µL RIPA lysis buffer with quenchers (50 mM Tris pH 7.4, 150 mM NaCl, 0.1% (w/v) SDS, 0.5% (w/v) sodium deoxycholate, 1% (v/v) Triton X-100, 10 mM sodium ascorbate, 5 mM Trolox, 10 mM sodium azide, 1 mM PMSF). Cells were disrupted using a Tissue lyser (Qiagen) with glass beads (0.1 mm) at a frequency of 30 Hz, with 30 cycles of 1 min on and 1 min off on ice. The lysate and beads were pelleted at 2,000 × g for 10 min at 4 °C and the supernatant was collected. Lysates were cleared by centrifugation at 12,000 x g for 10 min at 4 °C. Supernatant was transferred to a new tube and flash frozen. Total protein was estimated using the Pierce BCA protein assay.  Pierce streptavidin magnetic beads were washed twice in RIPA lysis buffer (50 mM Tris pH 7.4, 150 mM NaCl, 0.1% (w/v) SDS, 0.5% (w/v) sodium deoxycholate, 1% (v/v) Triton X-100) and the supernatant was removed. 800 µL of RIPA lysis buffer with quenchers containing 50 µg of protein for every 20 µL of streptavidin magnetic beads was added. Beads were incubated with protein for 1 h at RT on a rotator. The beads were then washed twice with RIPA lysis buffer, once with 1 M KCl, once with 0.1 M Na2CO3, once with 8 M urea in 10 mM Tris pH 7.5, and once again with RIPA lysis buffer. Biotinylated proteins were eluted from the beads by boiling each sample in in 22.5 µL of 2X Laemmli buffer supplemented with 2 mM biotin and 20 mM DTT for 15 min. The eluate was collected and diluted with 22.5 µL of water to run on gels. Proteins were separated on Any kD Mini-PROTEAN TGX precast gels (Bio-Rad) and stained using the Pierce silver stain kit (Thermo Fisher Scientific). Enriched biotinylated proteins by magnetic streptavidin beads were separated on Any kD Mini-PROTEAN TGX precast gels (Bio-Rad) and stained with Coomassie Brilliant Blue R-250 (Fisher Scientific). Lanes for each replicate were manually cut. Each band was destained with 10% methanol/5% glacial acetic acid (v/v). Gel bands were dehydrated using 100% acetonitrile and incubated with 10 mM dithiothreitol in 100 mM ammonium bicarbonate, pH ~8, at 56 °C for 45 min, dehydrated again and incubated in the dark with 50 mM iodoacetamide in 100 mM ammonium bicarbonate for 20 min. Gel bands were then washed with ammonium bicarbonate and dehydrated again. Sequencing grade modified trypsin was prepared to 0.005 µg µL-1 in 50 mM ammonium bicarbonate and ~100 µL of this was added to each gel band so that the gel was completely submerged. Bands were then incubated at 37 °C overnight. Peptides were extracted from the gel by water bath sonication in a solution of 60% acetonitrile/1% trifluoroacetic acid (v/v) and vacuum dried to ~2 µL. All samples were re-constituted in 20 µL of 2% acetonitrile/0.3% trifluoroacetic acid (v/v) and an injection of 5 µL (10 µL for bead samples) was automatically made using a using an Easy-nLC 1000 system (Thermo Fisher Scientific) onto an Acclaim PepMap RSLC 0.1 mm x 20 mm C18 trapping column (Thermo Fisher Scientific) and washed for ~5 min with buffer A. Bound peptides were then eluted over 35 min onto an Acclaim PepMap RSLC 0.075 mm x 250 mm resolving column (Thermo Fisher Scientific,) with a gradient of 5% buffer B to 38% buffer B in 24 min, ramping to 90% buffer B at 25 min and held at 90% buffer B for the duration of the run (buffer A = 99.9% water/0.1% formic acid (v/v), buffer B = 80% acetonitrile/0.1% formic acid/19.9% water (v/v)) at a constant flow rate of 300 nL min-1. Column temperature was maintained at a constant temperature of 50 °C using and integrated column oven (PRSO-V1, Sonation GmbH, Biberach). Eluted peptides were sprayed into a Q-Exactive mass spectrometer (Thermo Fisher Scientific,) using a FlexSpray spray ion source. Survey scans were taken in the Orbitrap (70000 resolution, determined at m/z 200) and the top 15 ions in each survey scan are then subjected to automatic higher energy collision induced dissociation with fragment spectra acquired at 17,500 resolution. The resulting MS/MS spectra were converted to peak lists using Mascot Distiller v2.8.1 and searched against a database containing all S. elongatus protein sequences available from Uniprot."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MaxQuant/Andromeda (version 2.0.3.1) was used to process raw files from the Q-Exactive mass spectrometer and search the peak lists against a database consisting of Uniprot S. elongatus proteome (UP000002717, total 2,657 entries, downloaded at 9/12/2021). Enzyme specificity was set as full cleavage by trypsin with two maximum missed cleavage sites permitted. Carbamidomethylation (Cys) was set as fixed modification, whereas dynamic modifications were set as oxidation (Met), deamidation (Asn/Gln), and acetylation (Protein N-terminal). MaxQuant used 4.5 ppm main search tolerance for precursor ions, 20 ppm MS/MS match tolerance, searching top 12 peaks per 100 Da. FDRs for both protein and peptide were 0.01 with a minimum of seven amino acid peptide length, and the minimum score for peptides was set to >40.Label-free quantification was enabled with minimum 2 LFQ ratio counts and a fast LFQ option. LFQ values were log2 transformed and missing intensity values were imputed using the “min” method, which replaces the missing values by the smallest non-missing value in the data set. Only proteins with at least two unique peptides and two spectral counts were considered identified in an individual sample. S. elongatus proteins identified in both CscB-SPS replicates and/or both Protein-APEX2 replicates were used for relative quantification. The log2 ratio of the MaxQuant LFQ intensities was used as metrics to determine enrichment in the Protein-APEX2 samples over the CscB-SPS sample (log2 LFQ Protein-APEX2/CscB-SPS). Unpaired two-sided Student’s t-tests were performed to determine the statistical significance between the CscB-SPS (control) and Protein-APEX2 samples. Proteins were considered to be proximity interactors when log2 LFQ Protein-APEX2/CscB-SPS was >1.5 and p-value in an unpaired Student’s t-test was <0.05. The Pearson coefficient correlation (r) was used to assess the similarities of quantified proteomes across samples."],"omics_type":["Proteomics"],"labhead":["Daniel Ducat"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, United States. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, United States."],"species":["Synechococcus Elongatus (strain Pcc 7942) (anacystis Nidulans R2)"],"publication":["10.1016/J.YMBEN.2023.11.001"],"submitter_mail":["santosm7@msu.edu"],"submitter_affiliation":["Michigan State University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a two-component signaling network implicated in organic carbon balancing in Synechococcus elongatus PCC 7942","description":"Photosynthetic organisms need to balance the rate of photosynthesis (source activity) with the utilization of photosynthetic products by downstream reactions (sink capacity). However, cyanobacteria lack homologs to the regulatory source/sink systems well-studied in plants, making it uncertain how they sense integrated metabolic demands to coordinate upstream photosynthetic reactions to meet those energetic needs. Towards the identification of energy/sugar sensors in cyanobacteria, we utilized an engineered strain of Synechococcus elongatus PCC 7942 with a heterologous sucrose export pathway that provides an expanded and tunable metabolic sink. We conducted a comprehensive screening all two-component systems (TCS) encoded in S. elongatus by analyzing phenotypes consistent with sucrose export-induced relaxation of sink inhibition (e.g., increased photosynthetic efficiencies) in TCS knockout backgrounds. We further narrowed candidate sensor proteins by analyzing the changes observed after sucrose feeding experiments in a strain with a heterologous transporter installed, akin to classic sugar feeding experiments in plants. Taken together, we show that a clustered TCS network containing RpaA, CikB, ManS and NblS are involved in the regulation of genes related to photosynthesis, pigment synthesis, and Rubisco concentration in response to sucrose export and feeding. Analysis of the protein-protein interactome of each of these factors by proximity labeling demonstrated enrichment of enzymes involved in core metabolism and energy production. Altogether, these results highlight a regulatory TCS group that may be playing under-appreciated functions in energy balancing in photosynthetically-active cyanobacteria.","dates":{"publication":"2026-05-29","submission":"2022-09-14"},"accession":"PXD036717","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:109376","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:305400","NEWT:1310161","NEWT:1230383","NEWT:77133","NCBITaxon:5207","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:32224","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:37919","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:65125","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2709072","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:367737","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","NEWT:29466","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055"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