{"refrec":{"BRefID":334903,"RR":"<b>Behnke, J.; Cohen, A.M.; LaRoche, J.</b> (2021). N-linked glycosylation enzymes in the diatom <i>Thalassiosira oceanica</i> exhibit a diel cycle in transcript abundance and favor for NXT-type sites. <i>NPG Scientific Reports 11(1)</i>: 3227. <a href=\"https://dx.doi.org/10.1038/s41598-021-82545-1\" target=\"_blank\">https://dx.doi.org/10.1038/s41598-021-82545-1</a>","BEntID":331460,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>NPG Scientific Reports 11(1)</i>: 3227. <a href=\"https://dx.doi.org/10.1038/s41598-021-82545-1\" target=\"_blank\">https://dx.doi.org/10.1038/s41598-021-82545-1</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Behnke, J.; Cohen, A.M.; LaRoche, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Behnke, J.; Cohen, A.M.; LaRoche, J.","Englishabstract":"N-linked glycosylation is a posttranslational modification affecting protein folding and function. The N-linked glycosylation pathway in algae is poorly characterized, and further knowledge is needed to understand the cell biology of algae and the evolution of N-linked glycosylation. This study investigated the N-linked glycosylation pathway in Thalassiosira oceanica, an open ocean diatom adapted to survive at growth-limiting iron concentrations. Here we identified and annotated the genes coding for the essential enzymes involved in the N-linked glycosylation pathway of T. oceanica. Transcript levels for genes coding for calreticulin, oligosaccharyltransferase (OST), N-acetylglucosaminyltransferase (GnT1), and UDP-glucose glucosyltransferase (UGGT) under high- and low-iron growth conditions revealed diel transcription patterns with a significant decrease of calreticulin and OST transcripts under iron-limitation. Solid-phase extraction of N-linked glycosylated peptides (SPEG) revealed 118 N-linked glycosylated peptides from cells grown in high- and low-iron growth conditions. The identified peptides had 81% NXT-type motifs, with X being any amino acids except proline. The presence of N-linked glycosylation sites in the iron starvation-induced protein 1a (ISIP1a) confirmed its predicted topology, contributing to the biochemical characterization of ISIP1 proteins. Analysis of extensive oceanic gene databases showed a global distribution of calreticulin, OST, and UGGT, reinforcing the importance of glycosylation in microalgae.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"N-linked glycosylation enzymes in the diatom <i>Thalassiosira oceanica</i> exhibit a diel cycle in transcript abundance and favor for NXT-type sites","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-15 01:33:29.819449","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2021,"MonPub":null,"DateUpdate":"2021-03-16","DateCreate":"2021-03-16","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000617534800002","VABBcode":null,"OpenAcc":1,"DOI":"10.1038/s41598-021-82545-1"},"refs":null,"anarec":{"AnaID":334903,"PubliDate":2021,"Pagination":"3227","XtraPublOfAnaID":null,"ISBN":null,"Volume":"11","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":208093,"SerRR":"Scientific Reports (Nature Publishing Group). 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