scholarly journals The Arabidopsis Somatic Embryogenesis Receptor Kinase 1 Gene Is Expressed in Developing Ovules and Embryos and Enhances Embryogenic Competence in Culture

2001 ◽  
Vol 127 (3) ◽  
pp. 803-816 ◽  
Author(s):  
Valérie Hecht ◽  
Jean-Philippe Vielle-Calzada ◽  
Marijke V. Hartog ◽  
Ed D.L. Schmidt ◽  
Kim Boutilier ◽  
...  
Keyword(s):  
Somatic Embryogenesis ◽  
Receptor Kinase ◽  
Embryogenic Competence ◽  
Somatic Embryogenesis Receptor Kinase

Expression of the Daucus carota somatic embryogenesis receptor kinase (DcSERK) protein in insect cells

Biochimie ◽  
2001 ◽  
Vol 83 (5) ◽  
pp. 415-421 ◽  
Author(s):  
Khalid Shah ◽  
Ed D.L. Schmidt ◽  
Just M. Vlak ◽  
Sacco C. de Vries
Keyword(s):  
Somatic Embryogenesis ◽  
Daucus Carota ◽  
Insect Cells ◽  
Receptor Kinase ◽  
Somatic Embryogenesis Receptor Kinase

Subcellular Localization and Oligomerization of the Arabidopsis thaliana Somatic Embryogenesis Receptor Kinase 1 Protein

2001 ◽  
Vol 309 (3) ◽  
pp. 641-655 ◽  
Author(s):  
Khalid Shah ◽  
Theodorus W.J. Gadella Jr ◽  
Harrie van Erp ◽  
Valérie Hecht ◽  
Sacco C. de Vries
Keyword(s):  
Arabidopsis Thaliana ◽  
Somatic Embryogenesis ◽  
Subcellular Localization ◽  
Receptor Kinase ◽  
Somatic Embryogenesis Receptor Kinase

scholarly journals Identification of Serk Gene from Bract Derived Embryogenic and Non - Embryogenic Calli of Four Diploid Banana Cultivars from South India

2017 ◽  
Vol 5 (4) ◽  
pp. 161
Author(s):  
Smitha P D ◽  
Binoy K R ◽  
Ashalatha S Nair
Keyword(s):  
Somatic Embryogenesis ◽  
Somatic Embryos ◽  
Cell Formation ◽  
Molecular Size ◽  
Receptor Kinase ◽  
Embryogenic Calli ◽  
Embryogenic Cell ◽  
Diploid Banana ◽  
Somatic Embryogenesis Receptor Kinase ◽  
Similar Intensity

Somatic embryogenesis receptor kinase (SERK) gene is known to be a marker of somatic embryogenesis in several plant species. The present study reported the presence of SERK gene from bract derived embryogenic calli bearing somatic embryos. The analysis of the expression pattern of the SERK gene during embryogenic cell formation and somatic embryogenesis revealed that SERK expression continued during pro embryogenic mass formation. In the present study the amplified product of cDNA from the somatic embryos has molecular size 1459 bp. The non- embryogenic callus also showed the presence of faint bands. In all the samples the amplified product from β - actin primer showed bands of 650 bp with similar intensity in both the embryogenic and non- embryogenic samples.

scholarly journals Molecular cloning and in silico analysis of three somatic embryogenesis receptor kinase mRNA from date palm

Genetika ◽  
2013 ◽  
Vol 45 (3) ◽  
pp. 837-853 ◽  
Author(s):  
Imen Rekik ◽  
Amine Elleuch ◽  
Walid Kriaa ◽  
Noureddine Drira
Keyword(s):  
Somatic Embryogenesis ◽  
Transmembrane Domain ◽  
In Silico Analysis ◽  
Kinase Domain ◽  
Variable Number ◽  
Open Reading Frames ◽  
Receptor Kinase ◽  
Ligand Binding Sites ◽  
Rapid Amplification ◽  
Somatic Embryogenesis Receptor Kinase

We report here the isolation and characterizations of three somatic embryogenesis receptor kinase (PhSERK) genes from palm date by a rapid amplification of cDNA ends (RACE) approach. PhSERKs belong to a small family of receptor kinase genes, share a conserved structure and extensive sequence homology with previously reported plant SERK genes. Sequence analysis of these genes revealed the sequence size of 11051 pb (PhSERK1), 7981 pb (PhSERK2) and 10510 pb (PhSERK3). The open reading frames of PhSERK1, PhSERK2 and PhSERK3 are 1914 pb, 1797 pb and 1719 pb respectively. PhSERKs belongs to the LRR-type cell surface RLKs, which possess a number of characteristic domains. These include an extracellular domain (EX) containing a variable number of LRR units, signal pepetide (SP) immediately followed by a single transmembrane domain (TM) and an intracellular kinase domain. The phylogenetic tree shows that the protein PhSERK1, PhSERK2 and PhSERK3 clustered within monocots SERKs proteins groups. We also predicted the secondary and tertiary with ligand binding sites structure of the protein PhSERKs.

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