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1.
Plant Biol (Stuttg) ; 6(4): 408-14, 2004 Jul.
Article in English | MEDLINE | ID: mdl-15248123

ABSTRACT

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.


Subject(s)
Carrier Proteins/genetics , Carrier Proteins/metabolism , Membrane Transport Proteins , Plant Proteins/genetics , Plant Proteins/metabolism , Sulfates/metabolism , Zea mays/metabolism , Base Sequence , Biological Transport, Active , Cloning, Molecular , DNA, Complementary/genetics , DNA, Plant/genetics , In Situ Hybridization , Molecular Sequence Data , Oxidoreductases Acting on Sulfur Group Donors/genetics , Oxidoreductases Acting on Sulfur Group Donors/metabolism , Phylogeny , Plant Roots/metabolism , Reverse Transcriptase Polymerase Chain Reaction , Sulfate Adenylyltransferase/genetics , Sulfate Adenylyltransferase/metabolism , Sulfate Transporters , Zea mays/genetics
2.
Biochim Biophys Acta ; 1350(2): 123-7, 1997 Feb 07.
Article in English | MEDLINE | ID: mdl-9048879

ABSTRACT

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.


Subject(s)
Acetyltransferases/genetics , Arabidopsis/genetics , Arabidopsis/metabolism , Cysteine/biosynthesis , Genes, Plant , Multigene Family , Acetyltransferases/chemistry , Amino Acid Sequence , Arabidopsis/enzymology , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , DNA, Plant/genetics , Escherichia coli/genetics , Escherichia coli/metabolism , Genetic Complementation Test , Molecular Sequence Data , Molecular Weight , Mutation , Open Reading Frames , Sequence Homology, Amino Acid , Serine O-Acetyltransferase
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