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Scholz"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Petd","Phosphorylation","Stt7","Chlamydomonas"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD060640"],"tissue":["Photosynthetic Cell"],"sample_protocol":["Protein isolation from cell pellets was carried out as described (Younas, M., Scholz, M., Marchetti, G. M. & Hippler, M. Remodeling of algal photosystem I through phosphorylation. Biosci Rep 43 (2023)). Reduction/alkylation of cysteines and tryptic digestion of proteins (100 µg per sample) was performed following the SP4 protocol (Johnston, H. E. et al. Solvent Precipitation SP3 (SP4) Enhances Recovery for Proteomics Sample Preparation without Magnetic Beads. Anal Chem 94, 10320-10328 (2022)) . After digestion, peptides were desalted using PurePep H50 SPE Spin columns (Affinisep). The peptide samples were divided into two aliquots: 5 µg for whole proteome analysis and 95 µg for phosphopeptide enrichment. Both aliquots were dried using vacuum centrifugation before further processing. To enrich phosphopeptides, titanium dioxide (TiO2) beads with 5 µm particle size (Titansphere, GL Sciences) in a metal oxide affinity chromatography (MOAC) procedure were used. TiO2 (1 mg per sample) was activated once with acetonitrile and equilibrated three times with loading buffer (LB; 80% (v/v) acetonitrile/5% (v/v) TFA/1 M glycolic acid). Loading buffer was added to create a 10% (w/v) TiO2 suspension. Peptide samples were dissolved in 50 µl LB, combined with 10 µl TiO2 suspension, and incubated for 30 minutes at 25°C in an Eppendorf Thermomixer at 1,200 rpm). The mixture was transferred to SDB-XC STAGE tips prepared in-house 45. Unless stated otherwise, all subsequent washing and elution steps were performed using 60 µl buffer volumes with in-between centrifugation at 2000 × g at room temperature. The buffer was removed by centrifugation and the TiO2 beads were washed twice with LB and once with 1% (v/v) acetonitrile/0.1% (v/v) TFA (W1). Non-phosphorylated peptides that were removed from the beads and subsequently bound to the SDB-XC membrane plug were removed by one wash with 80% (v/v) acetonitrile/0.1% (v/v) TFA (W2). The phosphopeptides were eluted from the TiO2 beads onto the SDB-XC material using 160 µl of pH 11 buffer (0.4 M sodium hydrogen phosphate/NaOH with 1% acetonitrile). After washing once with 1% acetonitrile/0.1% TFA, the phosphopeptides were sequentially eluted in three fractions using increasing concentrations of acetonitrile (7.5%, 20%, and 60%) in 100 mM ammonium formate (pH10). For samples from the STT7 experiment, only one fraction (60% acetonitrile in 100 mM ammonium formate (pH10)) was collected. The strongly bound phosphopeptides were eluted in two steps: first from the TiO2 beads using 5% ammonia, then from the SDB-CX membrane using 60% acetonitrile in 100 mM ammonium formate at pH 10. All fractions were dried by vacuum centrifugation and stored at  80°C until MS analysis. Whole proteome analysis Dried peptide samples were reconstituted in 5 µl of 2% (v/v) acetonitrile/0.05% (v/v) TFA in LC/MS grade water. Samples were analyzed on an LC-MS/MS system consisting of an Ultimate 3000 NanoLC (Thermo Fisher Scientific) coupled via a Nanospray Flex ion source (Thermo Fisher Scientific) to a Q Exactive Plus mass spectrometer (Thermo Fisher Scientific). Peptides were concentrated on a trap column (Acclaim Pepmap C18, 5 × 0.3 mm, 3 µm particle size, Thermo Scientific) for 3 min using 4% (v/v) acetonitrile/0.05% (v/v) in LC/MS grade water at a flow rate of 10 µl/min. The trap column was operated in back-flush mode, allowing the transfer of peptides on a reversed-phase column (PepSep Fifty, 500 × 0.075 mm, 1.9 µm particle size, Bruker) for chromatographic separation. The eluents used were 0.1% (v/v) formic acid in LC/MS grade water (A) and 0.1% (v/v) formic acid/80% (v/v) acetonitrile in LC/MS grade water (B). The gradient was programmed as follows: 2.5% to 5% B over 5 min, 5% to 17.5% B over 47 min, 17.5% to 40% B over 105 min, 40% to 99% B over 10 min, and 99% B for 20 min. Flow rate was 250 nl/min. The mass spectrometer was operated in data-dependent acquisition (DDA) mod, alternating between one MS1 full scan and up to 12 MS2 scans. Full scans were acquired with the following settings: AGC target 3e6, MS1 resolution 70000, maximum injection time 50 ms, scan range: 350–1400 m/z. Settings for MS were: AGC target 5e4, resolution 17500, MS2 maximum injection time 80 ms, intensity threshold 1e4, normalized collision energy 27 (HCD)). Dynamic exclusion was set to ‘auto’, assuming a chromatographic peak width (FWHM) of 60 s.  Phosphoproteomic analysis Prior to analysis, dried peptide samples were reconstituted in 5 µl of 2% (v/v) acetonitrile/0.05% (v/v) TFA in LC/MS grade water. LC-MS/MS system, flow rate and eluent compositions were the same as described above. The gradient for peptide separation was as follows: 2.5% to 5% B over 5 min, 5% to 40% B over 92 min, 40% to 99% B over 10 min, and 99% B for 20 min. The mass spectrometer used the same DDA mode settings as the whole proteome analysis, with two changes: MS2 maximum injection time was increased to 120 ms, and dynamic exclusion was set to 45 s."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For quantitative phosphoproteome analysis, mass spectrometry raw data from nonenriched and enriched samples were searched using Fragpipe against a concatenated, non-redundant database containing Chlamydomonas reinhardtii protein sequences from v5.6 and v6.1 gene models (Phytozome 13, phytozome-next.jgi.doe.gov). In addition, the polypeptide sequences of mutated/tagged proteins were added to the database. Default 'LFQ-MBR' workflow settings were applied to data from whole proteome samples, while the 'LFQ-phospho' workflow was used for phosphopeptide samples. A false discovery rate of 1% was applied at both peptide and protein levels. Fragpipe output files containing peptide/protein identifications and quantitative data ('combined_modified_peptide.tsv' from enriched samples and 'combined_protein.tsv' from whole proteome samples) were reformatted using a custom Python script to ensure compatibility with Phospho-Analyst (v. 1.0.2), which was used for differential expression analysis 48: Missing values were imputed using the 'MinProb' function, and variance stabilizing transformation was applied to normalize phosphosite intensities. Since the whole proteome LFQ data was already normalized in Fragpipe, no additional normalization steps were needed. Phospho-Analyst automatically corrected phosphosite abundance changes for underlying protein levels. A phosphorylation site localization probability threshold of 0.33 was applied, and p-values were adjusted using the Benjamini-Hochberg method."],"omics_type":["Proteomics"],"labhead":["Michael Hippler"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["WWU Münster"],"species":["Chlamydomonas Reinhardtii"],"publication":["Not available"],"submitter_mail":["mscholz@uni-muenster.de"],"submitter_affiliation":["IBBP Muenster"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoproteomic analysis of Chlamydomonas PetD mutants","description":"The cytochrome b6f complex (b6f) links photosystem II and photosystem I in photosynthetic electron transfer and is distributed between appressed and non-appressed thylakoid membranes. It also activates the state-transition 7 kinase (STT7), which phosphorylates light-harvesting complex proteins, facilitating energy redistribution between photosystems to optimize their efficiency. To investigate the role of STT7-dependent phosphorylation at T4 in the N-terminal domain of the b6f subunit-IV (PetD), we generated several chloroplast mutants. The phosphomimic mutation PetD T4E blocks STT7 kinase activity since proteomics show the absence of STT7-dependent phosphorylation and the strain being locked in State 1, revealing a novel feedback regulation mechanism. The deletion of five N-terminal amino acids resulted in a comparable inhibition of STT7 activity; furthermore, the additional disruption of electron transfer underscores an additional crucial role of the PetD N-terminus in b6f function.","dates":{"publication":"2026-04-04","submission":"2025-02-10"},"accession":"PXD060640","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:253237","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185",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