• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Molecular cloning and expression in photosynthetic bacteria of a soybean cDNA coding for phytoene desaturase an enzyme of the carotenoid biosynthesis pathway.
【2h】

Molecular cloning and expression in photosynthetic bacteria of a soybean cDNA coding for phytoene desaturase an enzyme of the carotenoid biosynthesis pathway.

机译：大豆八氢番茄红素cDNA的分子克隆和在光合细菌中的表达该八氢番茄红素去饱和酶是类胡萝卜素生物合成途径的一种酶。

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。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Carotenoids are orange, yellow, or red photo-protective pigments present in all plastids. The first carotenoid of the pathway is phytoene, a colorless compound that is converted into colored carotenoids through a series of desaturation reactions. Genes coding for carotenoid desaturases have been cloned from microbes but not from plants. We report the cloning of a cDNA for pds1, a soybean (Glycine max) gene that, based on a complementation assay using the photosynthetic bacterium Rhodobacter capsulatus, codes for an enzyme that catalyzes the two desaturation reactions that convert phytoene into zeta-carotene, a yellow carotenoid. The 2281-base-pair cDNA clone analyzed contains an open reading frame with the capacity to code for a 572-residue protein of predicted Mr 63,851. Alignment of the deduced Pds1 peptide sequence with the sequences of fungal and bacterial carotenoid desaturases revealed conservation of several amino acid residues, including a dinucleotide-binding motif that could mediate binding to FAD. The Pds1 protein is synthesized in vitro as a precursor that, upon import into isolated chloroplasts, is processed to a smaller mature form. Hybridization of the pds1 cDNA to genomic blots indicated that this gene is a member of a low-copy-number gene family. One of these loci was genetically mapped using restriction fragment length polymorphisms between Glycine max and Glycine soja. We conclude that pds1 is a nuclear gene encoding a phytoene desaturase enzyme that, as its microbial counterparts, contains sequence motifs characteristic of flavoproteins.
机译：类胡萝卜素是存在于所有质体中的橙色，黄色或红色的光保护性颜料。该途径的第一个类胡萝卜素是八氢番茄红素，这是一种无色化合物，可通过一系列去饱和反应转化为有色类胡萝卜素。已经从微生物而非植物中克隆了编码类胡萝卜素去饱和酶的基因。我们报告了一个克隆的pds1 cDNA，一个大豆（Glycine max）基因，它基于使用光合细菌荚膜红细菌的互补测定法，编码一种酶，该酶催化将脱氢番茄红素转化为ζ-胡萝卜素的两种去饱和反应，黄色类胡萝卜素。分析的2281个碱基对cDNA克隆包含一个开放阅读框，该框具有编码预测的63,851先生的572个残基蛋白质的能力。推导的Pds1肽序列与真菌和细菌类胡萝卜素去饱和酶序列的比对揭示了几个氨基酸残基的保守性，包括可以介导与FAD结合的二核苷酸结合基序。 Pds1蛋白是作为前体在体外合成的，一旦导入分离的叶绿体中，就会加工成较小的成熟形式。 pds1 cDNA与基因组印迹的杂交表明该基因是低拷贝数基因家族的成员。使用Glycine max和大豆大豆之间的限制性片段长度多态性对这些基因座之一进行了遗传定位。我们得出的结论是，pds1是编码八氢番茄红素去饱和酶的核基因，它作为微生物的对应物，含有黄素蛋白的特征序列基序。

著录项

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