Reduction of adenosine-5′-phosphosulfate instead of 3′-phosphoadenosine-5′-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae

被引:40
作者
Abola, AP [1 ]
Willits, MG [1 ]
Wang, RC [1 ]
Long, SR [1 ]
机构
[1] Stanford Univ, Howard Hughes Med Inst, Dept Biol Sci, Stanford, CA 94305 USA
关键词
D O I
10.1128/JB.181.17.5280-5287.1999
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We have cloned and sequenced three genes from Rhizobium meliloti (Sinorhizobium meliloti) that are involved in sulfate activation for cysteine biosynthesis. Two of the genes display homology to the Escherichia coli cysDN genes, which code for an ATP sulfurylase (EC 2.7.7.4). The third gene has homology to the E. coli cysH gene, a 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase (EC 1.8.99.4), but has greater homology to a set of genes found in Arabidopsis thaliana that encode an adenosine-5'-phosphosulfate (APS) reductase. In order to determine the specificity of the R. meliloti reductase, the R. meliloti cysH homolog was histidine tagged and purified, and its specificity was assayed in vitro. Like the A. thaliana reductases, the histidine-tagged R. meliloti cysH gene product appears to favor APS over PAPS as a substrate, with a K-m for APS of 3 to 4 mu M but a K-m for PAPS of >100 mu M. In order to determine whether this preference for APS is unique to R. meliloti among members of the family Rhizobiaceae or is more widespread, cell extracts from R. leguminosarum, Rhizobium sp. strain NGR234, Rhizobium fredii (Sinorhizobium fredii), and Agrobacterium tumefaciens mere assayed for APS or PAPS reductase activity. Cell extracts from all four species also preferentially reduce APS over PAPS.
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页码:5280 / 5287
页数:8
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