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Wu Q.,Shandong Peanut Research Institute SPRI | Wang C.T.,Shandong Peanut Research Institute SPRI
Advanced Materials Research | Year: 2014

The PHD finger is a highly conserved structural domain in roles with regulating transcription and modification of chromatin structure. Forty-five PHD finger genes encoding PHD finger protein were identified from soybean (Glycine max) database. And sixty - four unique typical PHD finger domains were retrieved. NJ phylogenetic tree of all 64 PHD finger domains consisted of ten main clades (A-J). Subcellular localization analysis shows that Glyma06g33590.1, Glyma10g05080.1 and Glyma11g11720.1 may localize in Golgi body, chloroplast thylakoid membrane and mitochondrial inner membrane, respectively. The function of domain is loyal to the cause of protein situated in particular site of cell. Eight unique domains have been found concomitant with PHD domain in a certain protein. The cooperative relationship between diverse domains may important for particular biological event. © (2014) Trans Tech Publications, Switzerland. Source


Wang X.Z.,Shandong Peanut Research Institute SPRI | Tang Y.Y.,Shandong Peanut Research Institute SPRI | Wu Q.,Shandong Peanut Research Institute SPRI | Sun Q.X.,Shandong Peanut Research Institute SPRI | And 3 more authors.
Grasas y Aceites | Year: 2015

As compared with its normal oleate counterpart, high oleate peanuts have better storage quality and several health benefits, and are therefore preferred by peanut shellers and consumers. High oleate has now become one of the main breeding objectives of peanuts. Thus far, over 50 high oleate peanut cultivars have been registered. Yet high oleate peanut breeding relies heavily on a limited number of high oleate genotypes. In this paper, we reported, for the first time, high peanut oleate natural mutants with large seeds derived from an intersectional cross, which were identified with near infra-red spectroscopy and confirmed by gas chromatography. Sequencing of FAD2 from the high-oleic hybrids along with their normal oleate parents indicated that a 448G >A mutation in FAD2A coupled with a 441-442ins A or G in FAD2B together caused high oleate phenotypes in these peanut hybrids. © 2015 CSIC. Source


Wu Q.,Shandong Peanut Research Institute SPRI | Wang X.Z.,Shandong Peanut Research Institute SPRI | Tang Y.Y.,Shandong Peanut Research Institute SPRI | Sun Q.X.,Shandong Peanut Research Institute SPRI | And 2 more authors.
Engineering Technology, Engineering Education and Engineering Management - International Conference on Engineering Technology, Engineering Education and Engineering Management, ETEEEM 2014 | Year: 2015

Here, we report the existence of a parvulin protein that has a strong sequence homology with Arabidopsis thaliana parvulin. The sequences of cDNA and DNA of this novel peanut peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 were cloned successfully from Arachis hypogaea cultivar Ri Hua 1. The full length PPIases NIMA-interacting 4 cDNA of A. hypogaea contains a 438 bp open reading frame (ORF) that encodes 145 amino acids. The length of PPIases NIMA-interacting 4 gene was 1201 bp, with four exons and three introns. Primary structure analysis revealed that the molecular weight of the putative PPIases NIMA- interacting 4 protein is 15334.36 Da with a theoretical pI 9.39. The deduced amino-acid sequence of PPIases NIMA- interacting 4 (A. hypogaea cultivar Ri Hua 1) shared a homology with other reported species, such as 93.8% identity with Glycine max (XM_003527043.2), 93.1% identity with Vitis vinifera (XP_002284794.1), and 85.3% identity with Oryza sativa Japonica Group (NP_001063153.1). The expression of PPIases NIMA-interacting 4 transcript shows that PPIases NIMA-interacting 4 mRNA was expressed mainly in roots. The PPIases NIMA- interacting 4 was identified successfully from A. hypogaea in this study. It provides scientific material for enriching and improving the peptidyl-prolyl cis-trans isomerases database. © 2015 Taylor & Francis Group, London. Source


Wu Q.,Shandong Peanut Research Institute SPRI | Wang X.Z.,Shandong Peanut Research Institute SPRI | Tang Y.Y.,Shandong Peanut Research Institute SPRI | Yu H.T.,Shandong Peanut Research Institute SPRI | And 3 more authors.
Canadian Journal of Plant Science | Year: 2014

The ribosomal proteins have been shown to be important in plant polarity establishment, cell proliferation, leaf shape and auxin-related development. The RPL4 protein is crucial for the maintenance of ribosomal translational efficiency and fidelity. This study concerns the RPL4 gene from Arachis hypogaea. The full-length cDNA (1538 bp) of RPL4 consisted of an open-reading frame of 1221 bp encoding 406 amino acids. The genomic DNA sequence of RPL4 gene consisted of 1491 bp containing two exons and one 270-bp intron. The RPL4 mRNA transcript was mainly expressed in roots and leaves, and fewer signals were detected in stems. The sequence data revealed that RPL4 encoded a typical ribosomal protein L4/L1e domain. Phylogenetic analysis for genes encoding proteins showed that RPL4 were conserved within dicotyledonous and monocotyledonous plants. The ratios of nonsynonymous/synonymous substitution rate (ω=dN/dS) were analyzed. No sites were identified under positive selection. In the whole RPL4 sequence, dS greatly exceeded dN in all branches of the tree (dN/dS< < 1.0), indicating that functional constraints (purifying selection) have acted on RPL4 throughout evolution. The differences among plants and animals and Caenorhabditis elegans may indicate functional differentiation during species evolution. Source


Wu Q.,Shandong Peanut Research Institute SPRI | Wang X.,Shandong Peanut Research Institute SPRI | Yu H.,Shandong Peanut Research Institute SPRI | Ding Y.,Shandong Peanut Research Institute SPRI | And 4 more authors.
Lecture Notes in Electrical Engineering | Year: 2014

RPL15 is a component of the large ribosomal subunit 60S. The sequences of cDNA and DNA of RPL15 were cloned successfully from Arachis hypogaea cultivar Ri Hua 1. These two sequences were analyzed preliminarily. The full length RPL15 cDNA of A. hypogaea contains a 615-bp open reading frame (ORF) which encodes 204 amino acids. The length of RPL15 gene was 1383 bp with three exons and two introns. Primary structure analysis revealed that the molecular weight of the putative RPL15 protein is 24211.09 Da with a theoretical pI of 11.44. The deduced amino acid sequence of RPL15 (A. hypogaea cultivar Ri Hua 1) shared homology with other reported species. The expression of RPL15 transcript showed that RPL15 mRNA was expressed mainly in root. The cDNA of RPL15 was cloned successfully from A. hypogaea in this study. It provides scientific material for enriching and improving the RPL15 gene database. © Springer-Verlag Berlin Heidelberg 2014. Source

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