{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/db.protein-peptides.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/db.proteins.csv"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dusk_Soluble_MRCB_2.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dusk_Pellet_MRCB_3.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dawn_Pellet_MRCB_8.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dawn_Soluble_MRCB_7.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dusk_Pellet_MRCB_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dusk_Soluble_MRCB_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dawn_Pellet_MRCB_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Dawn_Soluble_MRCB_7.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074299/Raw_data_explained_for_GlgA_MS.docx"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mrust@uchicago.edu"],"submitter":["Michael Rust"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cyanobacteria","Circadian"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074299"],"sample_protocol":["Protein from supernatant and pellet fractions was chloroform methanol extracted, trypsin digested and TMT labeled. The TMT-labeled samples were fractionated and fractions were submitted for LC-MS/MS analysis on Fusion Tribrid Lumos Orbitrap (Thermo Fisher). Each sample was submitted for single LC-MS/MS experiment that was performed on a Fusion Lumos Tribrid Instrument (Thermo Fischer) equipped with EASY1000 HPLC pump Peptides were separated onto a 100 μm inner diameter microcapillary trapping column packed first with approximately 5 cm of C18 Reprosil resin (5 μm, 100 Å, Dr. Maisch GmbH, Germany) followed by analytical column ∼20 cm of Reprosil resin (1.8 μm, 200 Å, Dr. Maisch GmbH, Germany). Separation was achieved through applying a gradient from 5%–27% ACN in 0.1% formic acid over 180 min at 200 nL min−1. Electrospray ionization was enabled through applying a voltage of 3 kV using a home-made electrode junction at the end of the microcapillary picofrit column (New Objective, MA). The Lumos was operated in data-dependent mode for the mass spectrometry methods. The mass spectrometry survey scan was performed in the Orbitrap in the range of 395 –1,800 m/z at a resolution of 6 × 104, followed by the selection of the twenty most intense ions (TOP20) were subjected to HCD MS2 event in Orbitrap part of the instrument. The fragment ion isolation width was set to 0.7 m/z, AGC was set to 50,000, the maximum ion time was 100 ms, normalized collision energy was set to 37V and an activation time of 1 ms for each HCD MS2 scan."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data were submitted for analysis in Proteome Discoverer 2.1.0.83 (Thermo Scientific) software. Assignment of MS/MS spectra were performed using the Sequest HT algorithm by searching the data against a protein sequence database including all entries from the Uniprot S. Elongates database (SwissProt 1,257 and TrEMBL7, 367; 2015) and other known contaminants such as human keratins and common lab contaminants. Sequest HT searches were performed using a 20 ppm precursor ion tolerance and requiring each peptides N-/C termini to adhere with Trypsin protease specificity, while allowing up to two missed cleavages. 6-plex TMT tags on peptide N termini and lysine residues (+229.162932 Da) was set as static modifications while methionine oxidation (+15.99492 Da) and heavy Leucine (+6.0200 Da) was set as variable modification. A MS2 spectra assignment false discovery rate (FDR) of 1% on protein level was achieved by applying the target-decoy database search. Filtering was performed using a Percolator (64bit version, reference 1). For quantification, a 0.02 m/z window centered on the theoretical m/z value of each the six reporter ions and the intensity of the signal closest to the theoretical m/z value was recorded. Reporter ion intensities were exported in result file of Proteome Discoverer 2.1 search engine as an excel tables for TMT6plex outputs and MS1 based signal intensities were exported for SILAC type heavy Leucine quantitation searches. The total signal intensity across all peptides quantified was summed for each TMT channel, and all intensity values were adjusted to account for potentially uneven TMT labeling and/or sample handling variance for each labeled channel. Each TMT labeled set of samples was submitted for ERLIC separation. After digestion peptides were separated on Agilent (Santa Clara, CA) 1200 HPLC system using PolyWAX LP column (PolyLC, Columbia MD) 200x2.1 mm, 5 μm, 300A for ERLIC (Electrostatic Repulsion Hydrophilic Interaction Chromatography) chromatography. Peptides were separated across 70 min gradient from 0% buffer A (90% acetonitrile 0.1% acetic acid) to 75% buffer B (30% acetonitrile, 0.1% formic acid) with 20 fractions been collected by time. Each fraction was dried in SpeedVac (Eppendorf, Germany) and re-suspended in 0.1% formic acid solution before injection to mass spectrometry. Single LC-MS/MS experiment that was performed on Orbitrap Q Exactive Plus (Thermo, CA) equipped with 1200 Agilent (Santa Clara, CA) Nano HPLC pump. Peptides were separated onto a 150 μm inner diameter microcapillary trapping column packed first with approximately 3 cm of C18 Reprosil resin (5 μm, 100 Å, Dr. Maisch GmbH, Germany) followed by analytical column ∼20 cm of Reprosil resin (1.8 μm, 200 Å, Dr. Maisch GmbH, Germany). Separation was achieved through applying a gradient from 5%–27% ACN in 0.1% formic acid over 90 min at 200 nL min−1. Electrospray ionization was enabled through applying a voltage of 2 kV using a home-made electrode junction at the end of the microcapillary column and sprayed from fused silica pico tips (New Objective, MA). The Q Exactive Plus was operated in data-dependent mode for the mass spectrometry methods. The mass spectrometry survey scan was performed in the Orbitrap in the range of 395 –1,800 m/z at a resolution of 6 × 104, followed by the selection of the twenty most intense ions (TOP20) for HCD-MS2 fragmentation in the Orbitrap using a precursor isolation width window of 2 m/z, AGC setting of 10,000, and a maximum ion accumulation of 200 ms. Singly charged ion species were not subjected to HCD fragmentation. Normalized collision energy was set to 37 V and an activation time of 1 ms. Ions in a 10 ppm m/z window around ions selected for MS2 were excluded from further selection for fragmentation for 60 s. After extracting the TMT spectral counts from supernatant and pellet fractions of light and dark incubated sample, we defined the soluble fraction as the ratio of counts in the supernatant to the sum of both supernatant and pellet. To correct for possible systematic batch effects between the two replicates, we used linear regression to normalize data from the 2nd replicate to have the same intercept and slope as the 1st replicate on the day %supernatant vs. night %supernatant plot. We defined two thresholds to consider a protein as a dark-demixing: its soluble fraction must be > 80% at the end of the day and < 45% during the night. If a protein was detected in both replicates, we required that it pass these criteria in both datasets."],"omics_type":["Proteomics"],"labhead":["Michael J Rust"],"instrument_platform":[""],"labhead_affiliation":["Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL USA 60637"],"submission_type":["PARTIAL"],"species":["Synechococcus Elongatus (strain Pcc 7942) (anacystis Nidulans R2)","Bacteria"],"publication":["42063545 Burton LA, Pattanayak GK, Rust MJ. Rhythmic protein condensation in the circadian regulation of glycogen metabolism. iScience. 2026 29(5):115605 10.1016/j.isci.2026.115605"],"submitter_mail":["mrust@uchicago.edu"],"submitter_affiliation":["University of Chicago"],"submitter_country":["United States"],"pubmed_abstract":["Circadian rhythms are endogenously generated daily cycles in physiology that are closely tied to metabolism and can be found in all kingdoms of life. Because of their genetic simplicity, cyanobacteria provide a unique opportunity to uncover rhythmic mechanisms. In cyanobacteria, glycogen storage is highly rhythmic. Using a combination of mass spectrometry and live cell imaging, we find that the glycogen synthase enzyme (GlgA), is rhythmically condensed. The appearance of condensed foci of GlgA corresponds to inhibition of glycogen synthesis during morning hours, allowing storage to be coordinated with the demand for energy at dusk. Through mutational analysis, we show that the condensation status of GlgA is dictated by the state of the circadian clock rather than the amount of glycogen in the cell. These results reveal a model of circadian control of glycogen metabolism achieved through rhythmic spatial reorganization of a key enzyme."],"pubmed_title":["Rhythmic protein condensation in the circadian regulation of glycogen metabolism."],"pubmed_authors":["Burton Lily A LA, Pattanayak Gopal K GK, Rust Michael J MJ"],"additional_accession":[]},"is_claimable":false,"name":"Circadian Rhythms in Cyanobacterial Protein Condensation","description":"Circadian rhythms are endogenously generated daily cycles in physiology that are closely tied to metabolism and can be found in all kingdoms of life. In cyanobacteria, energy storage through glycogen metabolism is highly rhythmic, but the underlying mechanisms remain unclear. Here we find that the glycogen synthase enzyme, GlgA, is rhythmically condensed during growth in constant light. The appearance of condensed foci of GlgA corresponds to inhibition of glycogen synthesis during the morning hours allowing storage to be coordinated with the demand for energy at dusk. Through mutational analysis, we show that the condensation status of GlgA is dictated by the state of the circadian clock rather than the amount of glycogen in the cell. These results reveal a model of circadian control of glycogen metabolism achieved through rhythmic spatial reorganization of a key 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