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1.
Plant Cell ; 29(1): 129-143, 2017 01.
Artigo em Inglês | MEDLINE | ID: mdl-28062750

RESUMO

UDP-glucuronic acid (UDP-GlcA) is the precursor of many plant cell wall polysaccharides and is required for production of seed mucilage. Following synthesis in the cytosol, it is transported into the lumen of the Golgi apparatus, where it is converted to UDP-galacturonic acid (UDP-GalA), UDP-arabinose, and UDP-xylose. To identify the Golgi-localized UDP-GlcA transporter, we screened Arabidopsis thaliana mutants in genes coding for putative nucleotide sugar transporters for altered seed mucilage, a structure rich in the GalA-containing polysaccharide rhamnogalacturonan I. As a result, we identified UUAT1, which encodes a Golgi-localized protein that transports UDP-GlcA and UDP-GalA in vitro. The seed coat of uuat1 mutants had less GalA, rhamnose, and xylose in the soluble mucilage, and the distal cell walls had decreased arabinan content. Cell walls of other organs and cells had lower arabinose levels in roots and pollen tubes, but no differences were observed in GalA or xylose contents. Furthermore, the GlcA content of glucuronoxylan in the stem was not affected in the mutant. Interestingly, the degree of homogalacturonan methylation increased in uuat1 These results suggest that this UDP-GlcA transporter plays a key role defining the seed mucilage sugar composition and that its absence produces pleiotropic effects in this component of the plant extracellular matrix.


Assuntos
Proteínas de Arabidopsis/metabolismo , Arabidopsis/metabolismo , Complexo de Golgi/metabolismo , Proteínas de Transporte de Nucleotídeos/metabolismo , Polissacarídeos/metabolismo , Sementes/metabolismo , Arabidopsis/genética , Proteínas de Arabidopsis/genética , Parede Celular/genética , Parede Celular/metabolismo , Regulação da Expressão Gênica de Plantas , Immunoblotting , Microscopia Confocal , Mutação , Proteínas de Transporte de Nucleotídeos/genética , Pectinas/metabolismo , Plantas Geneticamente Modificadas , Sementes/genética , Açúcares de Uridina Difosfato/metabolismo
2.
J Cell Biochem ; 116(8): 1638-45, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-25704669

RESUMO

Plants can be severely affected by salt stress. Since these are sessile organisms, they have developed different cellular responses to cope with this problem. Recently, it has been described that bZIP17 and bZIP60, two ER-located transcription factors, are involved in the cellular response to salt stress. On the other hand, bZIP60 is also involved in the unfolded protein response (UPR), a signaling pathway that up-regulates the expression of ER-chaperones. Coincidentally, salt stress produces the up-regulation of BiP, one of the main chaperones located in this organelle. Then, it has been proposed that UPR is associated to salt stress. Here, by using insertional mutant plants on bZIP17 and bZIP60, we show that bZIP17 regulate the accumulation of the transcript for the chaperone BiP3 under salt stress conditions, but does not lead to the accumulation of UPR-responding genes such as the chaperones Calnexin, Calreticulin, and PDIL under salt treatments. In contrast, DTT, a known inducer of UPR, leads to the up-regulation of all these chaperones. On the other hand, we found that bZIP60 regulates the expression of some bZIP17 target genes under conditions were splicing of bZIP60 does not occur, suggesting that the spliced and unspliced forms of bZIP60 play different roles in the physiological response of the plant. Our results indicate that the ER-located transcription factors bZIP17 and bZIP60 play a role in salt stress but this response goes through a signaling pathway that is different to that triggered by the unfolded protein response.


Assuntos
Proteínas de Arabidopsis/genética , Arabidopsis/crescimento & desenvolvimento , Fatores de Transcrição de Zíper de Leucina Básica/genética , Chaperonas Moleculares/genética , Processamento Alternativo , Arabidopsis/metabolismo , Ditiotreitol/farmacologia , Regulação da Expressão Gênica de Plantas , Salinidade , Estresse Fisiológico , Resposta a Proteínas não Dobradas/efeitos dos fármacos
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