Functional characterization of gibberellin oxidases from cucumber, Cucumis sativus L.

2013 ◽  
Vol 90 ◽  
pp. 62-69 ◽  
Author(s):  
Maria João Pimenta Lange ◽  
Anja Liebrandt ◽  
Linda Arnold ◽  
Sara-Miriam Chmielewska ◽  
André Felsberger ◽  
...  
Keyword(s):  
Cucumis Sativus ◽  
Functional Characterization ◽  
Cucumis Sativus L

scholarly journals Functional characterization of cucumber (Cucumis sativus L.) Clade V MLO genes

2017 ◽  
Vol 17 (1) ◽  
Author(s):  
Jeroen A. Berg ◽  
Michela Appiano ◽  
Gerard Bijsterbosch ◽  
Richard G. F. Visser ◽  
Henk J. Schouten ◽  
...  
Keyword(s):  
Cucumis Sativus ◽  
Functional Characterization ◽  
Cucumis Sativus L

scholarly journals Introduction pages

2018 ◽  
Vol 47 (2) ◽  
pp. I-VIII
Author(s):  
Radu E. SESTRAS
Keyword(s):  
Cucumis Sativus ◽  
Poa Pratensis ◽  
Plant Root ◽  
Functional Characterization ◽  
Kentucky Bluegrass ◽  
Weed Species ◽  
Temporary Immersion System ◽  
Cucumis Sativus L ◽  
Avocado Fruit

Notulae Botanicae Horti Agrobotanici Cluj-Napoca (NBHA), Issue 2, Volume 47, 2019: The papers published in this issue Vol 47 No 2 (2019) represent new exciting researches in different topics of life science, respectively in plant science, horticulture, agronomy and crop science. Among the interesting articles we invite you to find news about temporary immersion system for micropropagation of tree species and plant root hair growth in response to hormones (reviews); sexual and vegetative propagation of Hypericum empetrifolium Willd. subsp. empetrifolium; cloning and functional characterization of CsUGD2 in cucumber (Cucumis sativus L.); potential transference of CP4 EPSPS to weed species from genetically modified Gossypium hirsutum in Northern Mexico; isolation and functional characterization of an AGAMOUS-LIKE 18 (AGL18) MADS-box gene from cucumber (Cucumis sativus L.); avocado fruit pulp transcriptomes in the after-ripening process; transcriptome sequencing of two Kentucky bluegrass (Poa pratensis L.) genotypes in response to heat stress etc. Notulae Botanicae Horti Agrobotanici Cluj-Napoca journal has moved to online-only publication at the start of 2017; beginning in 2019, the journal appears quarterly. At the same time, we maintain our standard publication, as printed form, with ‘classic’ style - volume, issue, pagination.

Identification and functional characterization of APRR2 controlling green immature fruit color in cucumber (Cucumis sativus L.)

2017 ◽  
Vol 83 (2) ◽  
pp. 233-243 ◽  
Author(s):  
Jianqing Jiao ◽  
Hanqiang Liu ◽  
Jia Liu ◽  
Mingming Cui ◽  
Jing Xu ◽  
...  
Keyword(s):  
Cucumis Sativus ◽  
Functional Characterization ◽  
Fruit Color ◽  
Cucumis Sativus L ◽  
Immature Fruit

scholarly journals Functional Characterization of the Promoter and Second Intron of CUM1 During Flower Development in Cucumber (Cucumis sativus L.)

2018 ◽  
Vol 4 (3) ◽  
pp. 103-110 ◽  
Author(s):  
Ran GU ◽  
Xiaofeng LIU ◽  
Wensheng ZHAO ◽  
Shuangshuang YAN ◽  
Linhan SUN ◽  
...  
Keyword(s):  
Cucumis Sativus ◽  
Flower Development ◽  
Functional Characterization ◽  
Cucumis Sativus L

scholarly journals cDNA Cloning and Characterization of a Gibberellin-Responsive Gene in Hypocotyls of Cucumis sativus L.

1996 ◽  
Vol 37 (5) ◽  
pp. 686-691 ◽  
Author(s):  
M. Chono ◽  
T. Yamauchi ◽  
S. Yamaguchi ◽  
H. Yamane ◽  
N. Murofushi
Keyword(s):  
Cucumis Sativus ◽  
Cdna Cloning ◽  
Cucumis Sativus L ◽  
Responsive Gene

scholarly journals Cloning and Functional Characterization of CsUGD2 in Cucumber (Cucumis sativus L.)

2018 ◽  
Vol 47 (2) ◽  
pp. 288-293
Author(s):  
Yitong DUAN ◽  
Shuocheng ZENG
Keyword(s):  
Glucose Dehydrogenase ◽  
Functional Characterization ◽  
Protein Alignment ◽  
Cucumis Sativus L ◽  
Irreversible Oxidation ◽  
Cucumber Fruit ◽  
Key Enzyme ◽  
Cucumber Roots

UGD gene encodes UDP-glucose dehydrogenase (UGD) which is a key enzyme in the biosynthesis of cell wall, and it catalyses the irreversible oxidation of UDP-glucose (UDP-Glc) into UDP-glucuronic acid (UDP-GlcA). In cucumber, the expression level of CsUGD2 genes was higher in phloem tissues of pedicel and fruit than that in stalk. This study investigated the function of CsUGD2 in cucumber by different methods. Structure analysis indicated that CsUGD2 gene only has an exon with a length of 1,443 bp. Protein alignment suggested that UGD protein was highly conservative in different species. Phylogenetic analysis showed that CsUGD2 protein and CmoUGD2 protein form a same clade which is far away from UGDs in Arabidopsis. Real-time fluorescence quantitative analysis of CsUGD2 in different tissues of cucumber in the same period showed that CsUGD2 expressed highest in the root of cucumber. When we transformed CsUGD2 into wild type Arabidopsis, the roots of transgenic plants were shorter and the flowering time was delayed.  These results suggested that CsUGD2 may play an important role in the development of cucumber roots and only act on the development of cucumber fruit when compared with other plants fruits. However, the role of CsUGD2 in regulating the growth and development process of cucumber need to further study.

Characterization of plasma membrane bound cation-stimulated ATPase isolated from the roots of Cucumis sativus

1988 ◽  
Vol 66 (7) ◽  
pp. 1470-1473 ◽  
Author(s):  
Abdul Razaque Memon
Keyword(s):  
Plasma Membrane ◽  
Cucumis Sativus ◽  
Direct Interaction ◽  
Monovalent Cation ◽  
Phase System ◽  
Plasma Membrane Atpase ◽  
Cucumis Sativus L ◽  
Membrane Bound ◽  
Cucumber Roots

A membrane fraction enriched with Mg2+- or Mn2+-dependent, monovalent cation stimulated ATPase was isolated from cucumber roots (Cucumis sativus L.) by an aqueous two-polymer phase system of Dextran T500 (6.5%, w/w) and polyethylene glycol (PEG) 3350 (6.5%, w/w) at pH 7.8. The ATPase activity associated with the upper PEG-rich fraction (plasma membrane) was characterized. The optimum pH for the activation by Mg2+ and Mn2+ was in the range 5.8–6.0. The activity was substrate specific for ATP. Kinetics with Mg2+ or Mn2+ followed a simple Michaelis–Menten relationship. The apparent Km for Mg2+ activation (0.60 mM) of the ATPase was about twice that of the apparent Km for Mn2+ (0.38 mM). ATPase was stimulated by monovalent cations and showed an order of cation preference of [Formula: see text]. Calcium inhibited the plasma membrane ATPase, apparently by a direct interaction with ATPase rather than by disrupting the MgATP2− complex.

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