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Registro Completo |
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
06/11/2020 |
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Data da última atualização: |
06/11/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
RODRIGUES, G. R.; PINTO, O. H. B.; SCHROEDER, L. F.; FERNANDES, G. da R.; COSTA, O. Y. A.; QUIRINO, B. F.; KURAMAE, E. E.; BARRETO, C. C. |
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Afiliação: |
Gisele Regina Rodrigues, Universidade Católica de Brasília; Otávio Henrique Bezerra Pinto, Universidade Católica de Brasília; Luís Felipe Schroeder, Universidade Católica de Brasília; Gabriel da Rocha Fernandes, Fundação Oswaldo Cruz; Ohana Yonara Assis Costa, Netherlands Institute of Ecology; BETANIA FERRAZ QUIRINO, CNPAE; Eiko Eurya Kuramae, Netherlands Institute of Ecology; Cristine Chaves Barreto, Universidade Católica de Brasília. |
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Título: |
Unraveling the xylanolytic potential of Acidobacteria bacterium AB60 from Cerrado soils. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
FEMS Microbiology Letters, v. 367, Issue 18, fnaa149, Sept. 2020. |
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Volume: |
367 |
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DOI: |
https://doi.org/10.1093/femsle/fnaa149 |
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Idioma: |
Inglês |
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Conteúdo: |
The presence of genes for glycosyl hydrolases in many Acidobacteria genomes indicates an important role in the degradation of plant cell wall material. Acidobacteria bacterium AB60 was obtained from Cerrado oligotrophic soil in Brazil, where this phylum is abundant. The 16S rRNA gene analyses showed that AB60 was closely related to the genera Occallatibacter and Telmatobacter. However, AB60 grew on xylan as carbon source, which was not observed in Occallatibacter species; but growth was not detected on medium containing carboxymethyl cellulose, as observed in Telmatobacter. Nevertheless, the genome analysis of AB60 revealed genes for the enzymes involved in cellulose as well as xylan degradation. In addition to enzymes involved in xylan degradation, α-L-rhamnosidase was detected in the cultures of AB60. Functional screening of a small-insert genomic library did not identify any clones capable of carboxymethyl cellulose degradation, but open reading frames coding α-L-arabinofuranosidase and α-L-rhamnosidase were present in clones showing xylan degradation halos. Both enzymes act on the lateral chains of heteropolymers such as pectin and some hemicelluloses. These results indicate that the hydrolysis of α-linked sugars may offer a metabolic niche for slow-growing Acidobacteria, allowing them to co-exist with other plant-degrading microbes that hydrolyze β-linked sugars from cellulose or hemicellulose backbones. |
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Palavras-Chave: |
AB60; Acidobacteria bacterium. |
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Thesagro: |
Bactéria; Bacteriologia do Solo; Cerrado; Genoma. |
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Thesaurus Nal: |
Acidobacteria; Alpha-L-rhamnosidase; Cellulases; Genomics; Xylanases. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02503naa a2200373 a 4500
001 2126343
005 2020-11-06
008 2020 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1093/femsle/fnaa149$2DOI
100 1 $aRODRIGUES, G. R.
245 $aUnraveling the xylanolytic potential of Acidobacteria bacterium AB60 from Cerrado soils.$h[electronic resource]
260 $c2020
300 $a367
490 $v367
520 $aThe presence of genes for glycosyl hydrolases in many Acidobacteria genomes indicates an important role in the degradation of plant cell wall material. Acidobacteria bacterium AB60 was obtained from Cerrado oligotrophic soil in Brazil, where this phylum is abundant. The 16S rRNA gene analyses showed that AB60 was closely related to the genera Occallatibacter and Telmatobacter. However, AB60 grew on xylan as carbon source, which was not observed in Occallatibacter species; but growth was not detected on medium containing carboxymethyl cellulose, as observed in Telmatobacter. Nevertheless, the genome analysis of AB60 revealed genes for the enzymes involved in cellulose as well as xylan degradation. In addition to enzymes involved in xylan degradation, α-L-rhamnosidase was detected in the cultures of AB60. Functional screening of a small-insert genomic library did not identify any clones capable of carboxymethyl cellulose degradation, but open reading frames coding α-L-arabinofuranosidase and α-L-rhamnosidase were present in clones showing xylan degradation halos. Both enzymes act on the lateral chains of heteropolymers such as pectin and some hemicelluloses. These results indicate that the hydrolysis of α-linked sugars may offer a metabolic niche for slow-growing Acidobacteria, allowing them to co-exist with other plant-degrading microbes that hydrolyze β-linked sugars from cellulose or hemicellulose backbones.
650 $aAcidobacteria
650 $aAlpha-L-rhamnosidase
650 $aCellulases
650 $aGenomics
650 $aXylanases
650 $aBactéria
650 $aBacteriologia do Solo
650 $aCerrado
650 $aGenoma
653 $aAB60
653 $aAcidobacteria bacterium
700 1 $aPINTO, O. H. B.
700 1 $aSCHROEDER, L. F.
700 1 $aFERNANDES, G. da R.
700 1 $aCOSTA, O. Y. A.
700 1 $aQUIRINO, B. F.
700 1 $aKURAMAE, E. E.
700 1 $aBARRETO, C. C.
773 $tFEMS Microbiology Letters$gv. 367, Issue 18, fnaa149, Sept. 2020.
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| 1. |  | KOCHIAN, L.; HOEKENGA, O.; MAGALHAES, J.; PINEROS, M.; ALVES, V.; MARON, L.; MASON, P.; GUIMARAES, C.; SCHAFFERT, R. Integrating genomic, molecular genetic and physiological approaches to identify plant aluminum tolerance genes and their associated physilogical mechanisms. In: INTERNATIONAL PLANT NUTRITION COLLOQUIUM, 15., 2005, Beijing, China. Proceedings... Beijing: Tsinghua University, 2005. p. 18-19.| Tipo: Artigo em Anais de Congresso |
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