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1.
Plant Biol (Stuttg) ; 6(4): 408-14, 2004 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-15248123

RESUMO

A high-affinity-type sulfate transporter (Group 1: ZmST1;1, Accession No. AF355602) has been cloned from maize seedlings by RT-PCR. Tissue and cell specific localisation of this sulfate transporter has been determined along the developmental gradient of the root and in leaves of different ages. In S-sufficient conditions there was uniform low expression of ZmST1;1 in the root and very low expression in the leaves. Increased mRNA abundance and sulfate influx capacity indicated that S-starvation increased ZmST1;1 expression in roots, especially at the top of the root (just behind the seed, the area possessing most laterals and root hairs) compared to the root tip. Similarly a group 2, probable low affinity-type sulfate transporter, ZmST2;1, and also ATP-sulfurylase and APS-reductase but not OAS(thiol)lyase were induced by S-starvation and showed highest expression in the upper section of the root. S-starvation increased root/shoot ratio by 20 % and increased root lateral length and abundance in the region closest to the root tip. As the increase in root proliferation was not as great as the increase in mRNA pools, it was clear that there was a higher cellular abundance of the mRNAs for sulfate transporters, ATP-sulfurylase, and APS-reductase in response to sulfur starvation. In the leaves, the sulfate transporters, ATP-sulfurylase and APS-reductase were induced by S-starvation with the most mature leaf showing increased mRNA abundance first. In situ hybridization indicated that ZmST1;1 was expressed in epidermal and endodermal cell layers throughout the root whilst OAS(thiol)lyase was highly expressed in the root cortex.


Assuntos
Proteínas de Transporte/genética , Proteínas de Transporte/metabolismo , Proteínas de Membrana Transportadoras , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Sulfatos/metabolismo , Zea mays/metabolismo , Sequência de Bases , Transporte Biológico Ativo , Clonagem Molecular , DNA Complementar/genética , DNA de Plantas/genética , Hibridização In Situ , Dados de Sequência Molecular , Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética , Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo , Filogenia , Raízes de Plantas/metabolismo , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Sulfato Adenililtransferase/genética , Sulfato Adenililtransferase/metabolismo , Transportadores de Sulfato , Zea mays/genética
2.
Biochim Biophys Acta ; 1350(2): 123-7, 1997 Feb 07.
Artigo em Inglês | MEDLINE | ID: mdl-9048879

RESUMO

A cDNA clone, Sat-52, encoding a novel isoform of serine acetyltransferase (EC 2.3.1.30) was isolated by functional complementation of an Escherichia coli cysE mutant defective in serine acetyltransferase. The 1158 base pair clone contains a full-length open reading frame encoding a deduced protein of 312 amino acids with an M(r) of 32.77 kDa. Northern analysis revealed a single transcript of ca 1.19 kb that did not increase in abundance under sulfate limitation. Genomic Southern hybridization suggests the presence of a single copy of the Sat-52 gene.


Assuntos
Acetiltransferases/genética , Arabidopsis/genética , Arabidopsis/metabolismo , Cisteína/biossíntese , Genes de Plantas , Família Multigênica , Acetiltransferases/química , Sequência de Aminoácidos , Arabidopsis/enzimologia , Sequência de Bases , Clonagem Molecular , DNA Complementar/genética , DNA de Plantas/genética , Escherichia coli/genética , Escherichia coli/metabolismo , Teste de Complementação Genética , Dados de Sequência Molecular , Peso Molecular , Mutação , Fases de Leitura Aberta , Homologia de Sequência de Aminoácidos , Serina O-Acetiltransferase
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