首页> 外文OA文献 >Characterization of the gene encoding the autotrophic ATP sulfurylase from the bacterial endosymbiont of the hydrothermal vent tubeworm Riftia pachyptila.
【2h】

Characterization of the gene encoding the autotrophic ATP sulfurylase from the bacterial endosymbiont of the hydrothermal vent tubeworm Riftia pachyptila.

机译:从热液喷管虫Riftia pachyptila的细菌内共生体编码自养ATP氧化酶的基因的表征。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

摘要

ATP sulfurylase is a key enzyme in the energy-generating sulfur oxidation pathways of many chemoautotrophic bacteria. The utilization of reduced sulfur compounds to fuel CO2 fixation by the still-uncultured bacterial endosymbionts provides the basis of nutrition in invertebrates, such as the tubeworm Riftia pachyptila, found at deep-sea hydrothermal vents. The symbiont-containing trophosome tissue contains high levels of ATP sulfurylase activity, facilitating the recent purification of the enzyme. The gene encoding the ATP sulfurylase from the Riftia symbiont (sopT) has now been cloned and sequenced by using the partial amino acid sequence of the purified protein. Characterization of the sopT gene has unequivocally shown its bacterial origin. This is the first ATP sulfurylase gene to be cloned and sequenced from a sulfur-oxidizing bacterium. The deduced amino acid sequence was compared to those of ATP sulfurylases reported from organisms which assimilate sulfate, resulting in the discovery that there is substantial homology with the Saccharomyces cerevisiae MET3 gene product but none with the products of the cysDN genes from Escherichia coli nor with the nodP and nodQ genes from Rhizobium meliloti. This and emerging evidence from other sources suggests that E. coli may be atypical, even among prokaryotic sulfate assimilators, in the enzyme it employs for adenosine 5'-phosphosulfate formation. The sopT gene probe also was shown to specifically identify chemoautotrophic bacteria which utilize ATP sulfurylase to oxidize sulfur compounds.
机译:ATP硫酸化酶是许多化学自养细菌产生能量的硫氧化途径中的关键酶。仍未培养的细菌内共生体利用还原的硫化合物为固定二氧化碳提供燃料,为深海热液喷口发现的无脊椎动物(如块茎裂谷裂R)提供​​了营养基础。含有共生体的滋养体组织含有高水平的ATP硫酸化酶活性,有助于最近对该酶的纯化。现在,已经使用纯化蛋白的部分氨基酸序列克隆了来自裂谷共生体(sopT)的编码ATP硫化酶的基因,并对其进行了测序。 sopT基因的表征已明确显示其细菌来源。这是第一个从硫氧化细菌克隆并测序的ATP硫酸化酶基因。将推导的氨基酸序列与同化硫酸盐的生物体报告的ATP硫酸化酶序列进行了比较,从而发现与酿酒酵母MET3基因产物具有基本同源性,但与大肠杆菌cysDN基因产物和苜蓿根瘤菌的nodP和nodQ基因。来自其他来源的这一新证据表明,即使在原核硫酸盐同化剂中,大肠杆菌也可能是非典型的,因为它使用的酶可形成5'-磷酸腺苷。还显示了sopT基因探针可特异性鉴定利用ATP硫化酶氧化硫化合物的化学自养细菌。

著录项

  • 作者

    Laue, B E; Nelson, D C;

  • 作者单位
  • 年度 1994
  • 总页数
  • 原文格式 PDF
  • 正文语种 en
  • 中图分类

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号