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Zhang"],"technology_type":["Data-dependent acquisition","Proteogenomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Non-aug translation initiation; n-terminally extended protein isoforms; n-terminal extensions (ntes); upstream translation initiation sites (utiss); proteogenomics; monocots and dicots","upstream translation initiation sites (utiss)","monocots and dicots","n-terminally extended protein isoforms","Non-aug translation initiation","n-terminal extensions (ntes)","proteogenomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD058528"],"tissue":["Plant Cell","Leaf"],"sample_protocol":["Plant materials and growth conditions Maize (Zea mays, B73 inbred line), rice (Oryza sativa L. ssp. japonica cv. Nipponbare), and soybean (Glycine max L., ZH13) plants were grown in a temperature- and light-controlled greenhouse. The growth conditions for maize were a 15-h light/9-h dark photoperiod with a 28/25 ℃ day/night air temperature, and samples were collected at the three-leaf stage. For rice, the growth conditions were a 12-h light/12-h dark photoperiod with a 28/25 ℃ day/night air temperature, and samples were collected on day 56. Soybean plants were grown under a 16-h light/8-h dark photoperiod with a 22/21 ℃ day/night air temperature, and samples were collected till the trifoliate leaves were fully expanded. Three replicates of leaf samples for three plant species were collected, frozen in liquid nitrogen, and stored at -80 ℃ before subsequent analysis.  Protein extraction  Total proteins from plant leaf samples were extracted as previously reported (54). In brief, the leaf tissues (1 g) from each species were pulverized in liquid nitrogen and the powder was precipitated in 10% (w/v) trichloroacetic acid/acetone solution containing 65 mM dithiothreitol (DTT) at -20 °C for 1 h. The solution was then centrifuged at 10,000×g at 4 ℃ for 45 min with the supernatant discarded. The precipitate was vacuum-dried and solubilized in 1/10 volumes of SDT buffer (4% [w/v] SDS, 100 mM DTT, and 150 mM Tris-HCl, pH 8.0). After a 3-min incubation in boiling water, the suspensions were ultrasonicated (80 w, ultrasonic 10 s/time, every 15 s, repeated 10 times) and incubated at 100 ℃ for 3 min. The extract was centrifuged at 12,000×g at 25 ℃ for 10 min, and the total protein contents were quantified using the bicinchoninic acid (BCA) Protein Assay Reagent (Sigma-Aldrich, USA). The supernatants were stored at -80 ℃ for further analysis. Protein digestion and peptide fractionation The FASP procedure was used to digest 250 μg per sample with trypsin (Promega Corporation, USA) as previously described (54). Following digestion, the peptide filtrate was fractionated by strong cation exchange (SCX) chromatography using an AKTA Purifier system (GE Healthcare, USA). The dried peptide mixture was reconstituted and acidified with 2 ml of buffer A (10 mM KH2PO4 in 25%[v/v] of ACN, pH = 2.7) and loaded onto a PolySULFOETHYL 4.6×100 mm column (5 µm, 200 Å, PolyLC Inc, USA). Peptides were eluted at a flow rate of 1 mL/min with buffer B (500 mM KCl, 10 mM KH2PO4 in 25% of ACN, pH 2.7) in a gradient of 0-10% (v/v) for 2 min, 10-20% (v/v) for 25 min, 20-45% (v/v) for 5 min, and 50-100% (v/v) for 5 min. The elution was monitored by absorbance at 214 nm, and fractions were collected every 1 min. The collected fractions were combined into 15 pools and desalted on C18 Cartridges (Empore SPE Cartridges C18 standard density, bed I.D. 7 mm, volume 3 ml, Sigma-Aldrich, Germany). Each fraction was concentrated by vacuum centrifugation and reconstituted in 40 µl of 0.1% (v/v) trifluoroacetic acid. All samples were stored at -80 °C for LC-MS/MS analysis.  Liquid chromatography-tandem mass spectrometry analysis  A Q-Exactive HF-X mass spectrometer coupled to the Easy nLC 1200 (Thermo Fisher Scientific, USA) was used to analyze the samples. A total of 2 μg peptide was loaded onto a C18-reversed phase column (25 cm long, 75 μm inner diameter) packed with 3 μm resin (EASY-Column Capillary Columns, Thermo Fisher Scientific, USA) in buffer A (2% [v/v] acetonitrile and 0.1% [v/v] formic acid) and separated with a linear gradient of buffer B (80% [v/v] acetonitrile and 0.1% formic acid) at a flow rate of 250 nL/min controlled by IntelliFlow technology over a duration of 90 min. MS data were acquired using the data-dependent acquisition (DDA) mode, dynamically selecting the top 10 most abundant precursor ions from the survey scan (m/z=300-1,800) for higher-energy collision dissociation (HCD) fragmentation. The determination of the target value was based on predictive Automatic Gain Control (pAGC). The dynamic exclusion duration was 25 s. Survey scans were acquired at a resolution of 70,000 (m/z=200), and the resolution for HCD spectra was set to 17,500 (m/z=200). The normalized collision energy was set at 30 eV, and the underfill ratio, specifying the minimum percentage of the target value likely to be reached at maximum fill time, was defined as 0.1%. The instrument operated with peptide recognition mode enabled. Triplicate experiments were conducted for each sample in MS."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Customized database construction The complete transcriptome sequences for the three plant species used in this study were obtained from the following available databases: Ensembl Plants (http://ftp.ensemblgenomes.org/pub/plants/release-41/fasta/zea_mays/) for maize, MSU Rice Genome Annotation Project (http://rice.uga.edu/pub/data/Eukaryotic_Projects/o_sativa/annotation_dbs/pseudomolecules/version_7.0/all.dir/) for rice, and the National Genomics Data Center (https://ngdc.cncb.ac.cn/gwh/Assembly/652/show) for soybean. Customized databases were constructed for each species as previously described (52). Briefly, the upstream in-frame AUG and seven near-cognate codons differing from AUG by a single nucleotide (CTG, TTG, GTG, ACG, ATC, ATA, and ATT) were searched in the 5' direction from the annotated AUG for each transcript. The search continued until an in-frame upstream stop codon was encountered or at the start of the transcript if no in-frame stop codon was present in the 5' UTRs. The selection of these seven near-cognate codons out of the total nine was based on their previously observed frequencies as natural non-AUG start codons and the higher initiation efficiencies compared to the remaining two codons (AGG and AAG) determined by various assays (46,55). All these searched uTISs were designated as the potential uTIS sites, and in silico translation was performed starting from these codons and ending at the annotated stop codon for each transcript. This progress generated a collection of N-terminally extended protein isoforms, serving as the customized database for subsequent identification of non-AUG translation initiation events in the MS experiment.  Identification of non-AUG translation initiation events by MaxQuant The MaxQuant software (v.1.6.1.10) (56) was used to analyze the MS/MS raw data. The MS/MS spectra were searched against the constructed customized databases for the three plant species. The initial search was set at a precursor mass window of 6 ppm. The search followed the trypsin enzymatic cleavage rule with a maximum of two missed cleavage sites allowed and a mass tolerance of 20 ppm for fragment ions. Carbamidomethylation of cysteines was defined as a fixed modification, and methionine oxidation was defined as a variable modification. The cutoff of global FDR was set to 0.01 for both peptide and protein identification. For each species, the resulting MS/MS data were searched against the corresponding customized database in conjunction with the remaining CDS-encoded proteins without NTEs using the MaxQuant. All identified peptides were relocated to the corresponding positions of the N-terminally extended protein isoform sequences in the database and mapped to their transcript locations. According to the mapping positions, peptides were categorized into three classes: peptides fully mapping to the NTE regions were defined as \"before\" peptides; peptides spanning the position of the translation site of annotated AUGs were defined as \"through\" peptides; peptides mapping to the coding regions were defined as \"after\" peptides. For all identified peptides, only those unique peptides that met the following criteria were retained for further analysis: (1) presented in at least two of the three replicates in MS experiment; (2) scores were higher than the threshold of 20. Those N-terminally extended protein isoforms in the customized database that were detected with through and/or before peptides were retained, and their corresponding transcripts were identified as undergoing non-AUG translation initiation events with NTEs."],"omics_type":["Proteomics"],"labhead":["Liuji Wu"],"instrument_platform":[""],"labhead_affiliation":["National Key Laboratory of Wheat and Maize Crop Science, Collaborative Innovation Center of Henan Grain Crops, College of Agronomy, Henan Agricultural University, China"],"submission_type":["PARTIAL"],"species":["Oryza Sativa (rice)","Zea Mays (maize)","Glycine Max"],"submitter_mail":["yqzhang0825@163.com"],"publication":["42011784 Zhang Y, Chang B, Wang S, Tian L, Zhao H, Luo W, Zhang H, Zhang S, Wu S, Wu L. Computational prediction-combined proteogenomics unveils widespread non-AUG translation initiation events in plants. Nucleic Acids Res. 2026 54(7):gkag303 10.1093/nar/gkag303"],"submitter_affiliation":["Henan Agricultural university"],"submitter_country":["China"],"pubmed_abstract":["Non-AUG translation initiation can generate N-terminally extended proteoforms, contributing to proteome complexity and regulatory diversity. While well characterized in mammals, its identification in plants remains limited, hindering both functional investigations and cross-species comparisons. Here, we applied a computational prediction-combined proteogenomic strategy to systematically explore non-AUG translation initiation events in the monocots maize and rice and the dicot soybean, identifying 879 transcripts potentially producing 3 938 N-terminally extended proteoforms. These events exhibited both conserved and lineage-specific mechanistic features, including stable RNA secondary structures flanking upstream translation initiation sites (uTISs), codon and sequence context preferences between monocot and dicot species, and a lack of evolutionary conservation. Plant N-terminal extensions were predicted to encode diverse targeting signals, implicating them in subcellular localization and functional diversification. Comparative analysis revealed both conserved trends and plant-specific features relative to humans. Collectively, this study provides a foundational resource and conceptual framework to advance understanding of plant non-AUG translation within a cross-kingdom evolutionary context. It also offers new opportunities to elucidate the roles of non-AUG translation in regulatory networks, proteome diversification, and adaptive biological functions across eukaryotic systems."],"pubmed_title":["Computational prediction-combined proteogenomics unveils widespread non-AUG translation initiation events in plants."],"pubmed_authors":["Zhang Yuqian Y, Chang Baiyang B, Wang Shunxi S, Tian Lei L, Zhao Huina H, Luo Weiwei W, Zhang Hanxue H, Zhang Shoudong S, Wu Shubiao S, Wu Liuji L"],"additional_accession":[]},"is_claimable":false,"name":"Computational prediction combined with proteogenomics unveils widespread non-AUG translation initiation events in plants","description":"Non-AUG translation initiation is crucial for regulating translation, which can generate N-terminally extended protein isoforms with diverse biological functions. However, a comprehensive view of non-AUG translation initiation events with N-terminal extensions (NTEs) across monocots and dicots remains limited. Here, we identified a total of 879 transcripts undergoing non-AUG translation initiation events with NTEs in maize, rice and soybean using a computational prediction-combined proteogenomic strategy. Over half the non-AUG initiated candidates had multiple putative upstream translation initiation sites (uTISs), with GUG being the most common uTIS, followed by CUG in monocots and AUU in the dicot. Sequence context analyses showed that these putative uTISs tended to have Kozak sequence and high AG content favoring initiation. Additionally, non-AUG initiated candidates had longer 5' untranslated regions (UTRs) across all species, whereas other transcript features showed contrasting trends between monocots and the dicot. Furthermore, non-AUG initiated candidates in maize were implicated in essential cellular processes and diverse functional signals were observed in the NTEs, suggesting their biological implications. This study provides a comprehensive landscape of the shared and distinct characteristics of non-AUG translation initiation between monocot and dicot plants, and highlights the complexity of genetic decoding in shaping the dynamic composition of plant proteomes.","dates":{"publication":"2026-04-27","submission":"2024-12-03"},"accession":"PXD058528","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:2042545","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:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:5535","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","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","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:1072569","NEWT:1072568","NEWT:161934","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:393133","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:550537","NEWT:284812","NEWT:284811","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:292415","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","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:936350","NEWT:1883446","NEWT:380703","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:175694","NEWT:1883456","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","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:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:1002697","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","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:630390","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:10835","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:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353154","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:5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