{"refrec":{"BRefID":312235,"RR":"<b>Bayer, B.; Pelikan, C.; Bittner, M.J.; Reinthaler, T.; Könneke, M.; Herndl, G.; Offre, P.</b> (2019). Proteomic response of three marine ammonia-oxidizing archaea to hydrogen peroxide and their metabolic interactions with a heterotrophic alphaproteobacterium. <i>mSystems 4(4)</i>: e00181-19. <a href=\"https://dx.doi.org/10.1128/msystems.00181-19\" target=\"_blank\">https://dx.doi.org/10.1128/msystems.00181-19</a>","BEntID":304599,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>mSystems 4(4)</i>: e00181-19. <a href=\"https://dx.doi.org/10.1128/msystems.00181-19\" target=\"_blank\">https://dx.doi.org/10.1128/msystems.00181-19</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Bayer, B.; Pelikan, C.; Bittner, M.J.; Reinthaler, T.; Könneke, M.; Herndl, G.; Offre, P.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Bayer, B. <i>et al.</i>","Englishabstract":"Ammonia-oxidizing archaea (AOA) play an important role in the nitrogen cycle and account for a considerable fraction of the prokaryotic plankton in the ocean. Most AOA lack the hydrogen peroxide (H<SUB>2</SUB>O<SUB>2</SUB>)-detoxifying enzyme catalase, and some AOA have been shown to grow poorly under conditions of exposure to H<SUB>2</SUB>O<SUB>2</SUB>. However, differences in the degrees of H<SUB>2</SUB>O<SUB>2</SUB> sensitivity of different AOA strains, the physiological status of AOA cells exposed to H<SUB>2</SUB>O<SUB>2</SUB>, and their molecular response to H<SUB>2</SUB>O<SUB>2</SUB> remain poorly characterized. Further, AOA might rely on heterotrophic bacteria to detoxify H<SUB>2</SUB>O<SUB>2</SUB>, and yet the extent and variety of costs and benefits involved in these interactions remain unclear. Here, we used a proteomics approach to compare the protein profiles of three <i>Nitrosopumilus</i> strains grown in the presence and absence of catalase and in coculture with the heterotrophic alphaproteobacterium Oceanicaulis alexandrii. We observed that most proteins detected at a higher relative abundance in H<SUB>2</SUB>O<SUB>2</SUB>-exposed <i>Nitrosopumilus</i> cells had no known function in oxidative stress defense. Instead, these proteins were putatively involved in the remodeling of the extracellular matrix, which we hypothesize to be a strategy limiting the influx of H<SUB>2</SUB>O<SUB>2</SUB> into the cells. Using RNA-stable isotope probing, we confirmed that O. alexandrii cells growing in coculture with the <i>Nitrosopumilus</i> strains assimilated <i>Nitrosopumilus</i>-derived organic carbon, suggesting that AOA could recruit H<SUB>2</SUB>O<SUB>2</SUB>-detoxifying bacteria through the release of labile organic matter. Our results contribute new insights into the response of AOA to H<SUB>2</SUB>O<SUB>2</SUB> and highlight the potential ecological importance of their interactions with heterotrophic free-living bacteria in marine environments.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Proteomic response of three marine ammonia-oxidizing archaea to hydrogen peroxide and their metabolic interactions with a heterotrophic alphaproteobacterium","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Nitrosopumilus; ammonia-oxidizing archaea; hydrogen peroxide; metabolic interactions; oxidative stress; proteomics","OtherDescriptors":null,"Notes":null,"AnaPub":2019,"MonPub":null,"DateUpdate":"2019-06-26","DateCreate":"2019-06-26","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000482629400006","VABBcode":null,"OpenAcc":1,"DOI":"10.1128/msystems.00181-19"},"refs":null,"anarec":{"AnaID":312235,"PubliDate":2019,"Pagination":"e00181-19","XtraPublOfAnaID":null,"ISBN":null,"Volume":"4","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":291446,"SerRR":"mSystems. 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