Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.

Winter AD; Keskiaho K; Kukkola L; McCormack G; Felix MA; Myllyharju J; Page AP

首页> 外文期刊>Matrix biology: Journal of the International Society for Matrix Biology >Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.

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Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.

机译：尽管线虫的氨基酸亚基序列相同，但两种线虫之间的胶原脯氨酰4-羟化酶组装差异。

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The collagen prolyl 4-hydroxylases (P4Hs) are essential for proper extracellular matrix formation in multicellular organisms. The vertebrate enzymes are alpha(2)beta(2) tetramers, in which the beta subunits are identical to protein disulfide isomerase (PDI). Unique P4H forms have been shown to assemble from the Caenorhabditis elegans catalytic alpha subunit isoforms PHY-1 and PHY-2 and the beta subunit PDI-2. A mixed PHY-1/PHY-2/(PDI-2)(2) tetramer is the major form, while PHY-1/PDI-2 and PHY-2/PDI-2 dimers are also assembled but less efficiently. Cloning and characterization of the orthologous subunits from the closely related nematode Caenorhabditis briggsae revealed distinct differences in the assembly of active P4H forms in spite of the extremely high amino acid sequence identity (92-97%) between the C. briggsae and C. elegans subunits. In addition to a PHY-1/PHY-2(PDI-2)(2) tetramer and a PHY-1/PDI-2 dimer, an active (PHY-2)(2)(PDI-2)(2) tetramer was formed in C. briggsae instead of a PHY-2/PDI-2 dimer. Site-directed mutagenesis studies and generation of inter-species hybrid polypeptides showed that the N-terminal halves of the Caenorhabditis PHY-2 polypeptides determine their assembly properties. Genetic disruption of C. briggsae phy-1 (Cb-dpy-18) via a Mos1 insertion resulted in a small (short) phenotype that is less severe than the dumpy (short and fat) phenotype of the corresponding C. elegans mutants (Ce-dpy-18). C. briggsae phy-2 RNA interference produced no visible phenotype in the wild type nematodes but produced a severe dumpy phenotype and larval arrest in phy-1 mutants. Genetic complementation of the C. briggsae and C. elegans phy-1 mutants was achieved by injection of a wild type phy-1 gene from either species.

机译：胶原蛋白脯氨酰4-羟基酶（P4Hs）对于在多细胞生物中正确形成细胞外基质至关重要。脊椎动物酶是alpha（2）beta（2）四聚体，其中的beta亚基与蛋白质二硫键异构酶（PDI）相同。已显示独特的P4H形式是由秀丽隐杆线虫催化的α亚基同种型PHY-1和PHY-2和β亚基PDI-2组装而成。混合的PHY-1 / PHY-2 /（PDI-2）（2）四聚体是主要形式，而PHY-1 / PDI-2和PHY-2 / PDI-2二聚体也被组装但效率较低。尽管近交线虫和秀丽隐杆线虫亚基之间的氨基酸序列同一性极高（92-97％），但从密切相关的线虫秀丽隐杆线虫的直系同源亚基的克隆和鉴定显示出活性P4H形式的装配存在明显差异。。除了PHY-1 / PHY-2（PDI-2）（2）四聚体和PHY-1 / PDI-2二聚体外，还有有源（PHY-2）（2）（PDI-2）（2）四聚体在梭状芽孢杆菌中形成而不是PHY-2 / PDI-2二聚体。定点诱变研究和种间杂合多肽的产生表明，秀丽隐杆线虫PHY-2多肽的N末端一半决定了它们的装配特性。通过Mos1插入对C. briggsae phy-1（Cb-dpy-18）的遗传破坏导致了一个小的（短）表型，没有相应的秀丽线虫C. elegans突变体（Ce）的矮胖（短和胖）表型严重。 -dpy-18）。 C. briggsae phy-2 RNA干扰在野生型线虫中未产生可见表型，但在phy-1突变体中产生了严重的矮胖表型和幼虫停滞。通过注射来自任何一个物种的野生型phy-1基因，可以实现Briggsae和秀丽隐杆线虫phy-1突变体的遗传互补。

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来源
《Matrix biology: Journal of the International Society for Matrix Biology》 |2007年第5期|共14页
作者
Winter AD; Keskiaho K; Kukkola L; McCormack G; Felix MA; Myllyharju J; Page AP;
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正文语种 eng
中图分类细胞生物学;
关键词
Carbon ion; Phenotype; Caenorhabditis; personal identity; Hydroxylases; 表型; 新杆状线虫; 羟化酶类;

机译：Carbon ion;Phenotype;Caenorhabditis;personal identity;Hydroxylases;表型;新杆状线虫;羟化酶类;

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1. Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits. [J] . Winter AD, Keskiaho K, Kukkola L, Matrix biology: Journal of the International Society for Matrix Biology . 2007,第5期

机译：尽管线虫的氨基酸亚基序列相同，但两种线虫之间的胶原脯氨酰4-羟化酶组装差异。
2. Prolyl 4-Hydroxylase Is an Essential Procollagen-Modifying Enzyme Required for Exoskeleton Formation and the Maintenance of Body Shape in the Nematode Caenorhabditis elegans [J] . Alan D. Winter, Antony P. Page Molecular and Cellular Biology . 2000,第11期

机译：Prolyl 4-羟化酶是线虫秀丽隐杆线虫外骨骼形成和维持体形所需的必需的胶原蛋白修饰酶。
3. Genetic interaction between Caenorhabditis elegans teneurin ten-1 and prolyl 4-hydroxylase phy-1 and their function in collagen IV-mediated basement membrane integrity during late elongation of the embryo [J] . Ulrike Topf, Ruth Chiquet-Ehrismann Molecular biology of the cell . 2011,第18期

机译：秀丽隐杆线虫teneurin ten-1和脯氨酰4-羟化酶phy-1之间的遗传相互作用及其在胚胎晚期伸长过程中胶原IV介导的基底膜完整性的功能
4. ConsDiff: identification of conserved differences between sets of amino acid sequences [C] . Mehta, S., Dinakarpandian, . 2003

机译：ConsDiff：鉴定氨基酸序列组之间的保守差异
5. Two studies in the nematode Caenorhabditis elegans: Part I. Gon-4: An organ-specific cell cycle regulator. Part II. Prolyl-4-hydroxylase: A critical enzyme required for morphology and viability. [D] . Friedman, Lisa Cheryl. 2000

机译：线虫秀丽隐杆线虫的两项研究：第一部分。Gon-4：一种器官特异性细胞周期调节剂。第二部分脯氨酰-4-羟化酶：形态和生存能力所必需的关键酶。
6. Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase. [O] . A Vuorela, J Myllyharju, R Nissi, 1997

机译：酵母毕赤酵母中人脯氨酰4-羟化酶和III型胶原蛋白的组装：稳定酶四聚体的形成需要与胶原蛋白共表达而稳定胶原蛋白的组装需要与脯氨酰4-羟化酶共表达。
7. Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits [O] . Winter, Alan D., Keskiaho, Katriina, Kukkalo, Liisa, 2007

机译：尽管酶亚基具有高氨基酸序列同一性，但两种线虫病线虫之间胶原蛋白脯氨酰4-羟化酶组装的差异

Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.

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