A novel sulfotransferase abundantly expressed in the dauer larvae of Caenorhabditis elegans
A novel sulfotransferase abundantly expressed in the dauer larvae of Caenorhabditis elegans
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DOI：
10.1093/jb/mvj041
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发表时间：
2006-03-01
影响因子：
2.7
通讯作者：
Tamura, H
中科院分区：
文献类型：
--
作者：
Hattori, K;Inoue, M;Tamura, H
我们从秀丽隐杆线虫中分离到一个基因（克隆Y113G7A.11）。elegans），我们将其命名为ceST 1，并且其是存在于该生物体基因组中的胞质磺基转移酶（SULT）基因家族的唯一成员。我们根据其推导的氨基酸序列鉴定了ceST 1的SULT基序，随后在大肠杆菌中表达了ceST 1 cDNA，并表征了其酶学性质。重组蛋白对4-硝基苯酚和2-萘酚底物具有硫酸化活性，但不催化单胺或羟基类固醇的硫酸化。另一种被ceST 1硫酸化的化合物是双酚A，已知双酚A刺激C中的生殖细胞增殖。优雅在C. elegans，可能是由于热不稳定抑制剂。ceST 1蛋白在C. elegans使用针对重组ceST 1产生的抗血清，并且在整个发育阶段也可以检测到转录物。此外，高水平的ceST 1的表达是明显的，在胚胎和成人阶段，并在dauer幼虫增强。这些发现表明，这种磺基转移酶要么形成对外源性物质的防御系统的一部分，要么调节C.优雅的
We have isolated a gene (clone Y113G7A.11) from Caenorhabditis elegans (C. elegans), that we have designated as ceST1, and which is the only member of the cytosolic sulfotransferase (SULT) gene family present in the genome of this organism. We identified the SULT motifs of ceST1 based upon their deduced amino acid sequence, and subsequently expressed the ceST1 cDNA in Escherichia coli and characterized its enzymatic properties. The recombinant protein showed sulfation activity for 4-nitrophenol and 2-naphthol substrates, but did not catalyze the sulfation of either monoamines or hydroxysteroids. Another compound sulfated by ceST1 is bisphenol A, which is known to stimulate germ cell proliferation in C. elegans. SULT activity was not detected in the cytosol of C. elegans, probably due to heat labile inhibitors. The ceST1 protein was detectable in the cytosol of C. elegans using anti-sera raised against recombinant ceST1, and transcripts could also be detected throughout the developmental stages. Moreover, high levels of ceST1 expression were evident at both the embryonic and adult stages and were augmented in dauer larva. These findings suggest that this sulfotransferase either forms part of a defence system against xenobiotics or regulates germ cell proliferation in C. elegans.