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  • 1
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    Archaea dominate oxic subseafloor communities over multimillion-year time scales (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉Ammonia-oxidizing archaea (AOA) dominate microbial communities throughout oxic subseafloor sediment deposited over millions of years in the North Atlantic Ocean. Rates of nitrification correlated with the abundance of these dominant AOA populations, whose metabolism is characterized by ammonia oxidation, mixotrophic utilization of organic nitrogen, deamination, and the energetically efficient chemolithoautotrophic hydroxypropionate/hydroxybutyrate carbon fixation cycle. These AOA thus have the potential to couple mixotrophic and chemolithoautotrophic metabolism via mixotrophic deamination of organic nitrogen, followed by oxidation of the regenerated ammonia for additional energy to fuel carbon fixation. This metabolic feature likely reduces energy loss and improves AOA fitness under energy-starved, oxic conditions, thereby allowing them to outcompete other taxa for millions of years.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Brazil's drought: protect biodiversity (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vitule, Jean Ricardo Simoes -- Azevedo-Santos, Valter M -- Daga, Vanessa Salete -- Lima-Junior, Dilermando Pereira -- de Magalhaes, Andre Lincoln Barroso -- Orsi, Mario Luis -- Pelicice, Fernando Mayer -- Agostinho, Angelo Antonio -- New York, N.Y. -- Science. 2015 Mar 27;347(6229):1427-8. doi: 10.1126/science.347.6229.1427-b. Epub 2015 Mar 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratorio de Ecologia e Conservacao (LEC), Universidade Federal do Parana, Curitiba, PR, 81531-970, Brazil. biovitule@gmail.com. ; Laboratorio de Ictiologia, Departamento de Zoologia, Universidade Estadual Paulista "Julio de Mesquita Filho," Campus de Botucatu, SP, 18618-970, Brazil. ; Laboratorio de Ecologia e Conservacao (LEC), Universidade Federal do Parana, Curitiba, PR, 81531-970, Brazil. ; Departamento de Ciencias Biologicas e da Saude, Universidade Federal do Mato Grosso, Campus Medio Araguaia, Pontal do Araguaia, MT, 78698-000, Brazil. ; Universidade Federal de Sao Joao Del Rei, Programa de Pos-Graduacao em Tecnologias para o Desenvolvimento Sustentavel, Ouro Branco, MG, 36420-000, Brazil. ; Museu de Zoologia, Departamento de Biologia Animal e Vegetal, Universidade Estadual de Londrina, Londrina, PR, 86051-990, Brazil. ; Nucleo de Estudos Ambientais, Universidade Federal de Tocantins, Porto Nacional, TO, 77500-000, Brazil. ; Nucleo de Pesquisas em Limnologia, Ictiologia e Aquicultura (NUPELIA)/DBI, UEM, Maringa, PR, 87020-900, Brazil.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25814574" target="_blank"〉PubMed〈/a〉
    Keywords: *Climate Change ; *Droughts ; Humans ; *Water Supply
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    A persulfidation-based mechanism controls aquaporin-8 conductance (2018)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2018-05-03
    Description: Upon engagement of tyrosine kinase receptors, nicotinamide adenine dinucleotide phosphate (NADPH)–oxidases release H 2 O 2 in the extracellular space. We reported previously that aquaporin-8 (AQP8) transports H 2 O 2 across the plasma membrane and is reversibly gated during cell stress, modulating signal strength and duration. We show that AQP8 gating is mediated by persulfidation of cysteine 53 (C53). Treatment with H 2 S is sufficient to block H 2 O 2 entry in unstressed cells. Silencing cystathionine β-synthase (CBS) prevents closure, suggesting that this enzyme is the main source of H 2 S. Molecular modeling indicates that C53 persulfidation displaces a nearby histidine located in the narrowest part of the channel. We propose that H 2 O 2 molecules transported through AQP8 sulfenylate C53, making it susceptible to H 2 S produced by CBS. This mechanism tunes H 2 O 2 transport and may control signaling and limit oxidative stress.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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