ISOLATION AND IDENTIFICATION OF A NEW PROTEIN FOR CAPPARIS SPINOSA RPS4 GENE

Authors

1 Biochemistry Department, Faculty of Science, Zagazig University, Egypt

2 BicChemistry Department, Faculty of Science, Ain-Shams University.

Abstract

Capparis spinosa is arangland plant species growing in the
desert of Egypt. It's one of the most important species in family
cappariecia. Capparis spinosa is one of the medicinal plants
established to have high diversity range of economic and medicinal
value. Recently, the pharmacology and chemistry of this plant have
been extensively studied. Chemical studies of the different parts of
Capparis, both fermented and non-fermented, have shown the
presence of many beneficial compounds. In this study the author
selected a 606bp ribosomal protein 4s (rps4) chloroplast gene of
Capparis spinosa, where the complete sequence of rps4 gene was
amplified, sequenced, cloned, and expressed. rps4 gene is a gene in
the land plant chloroplast genome and it is one of very popular
marker in this genome. The forward primer started with the start
codon ATG of rps4 and the reverse primer was designed to align
aregion of 18nt upstream of the stop codon. The isolated gene is
approximately 606 bp in lenght. After data alignment it was found
that maximum identity was 98% with Capparis flexuosa ribosoma
protein S4 (rps4) gene and 96% with Nasturtium officinale
ribosomal protein S4 (rps4) gene. The information of this gene was
found to be a new gene in comparison to the reported genes in the
gene bank. According to the gene bank it's a new gene. Therefore it
was given an accession number. The isolated gene was a complete
gene and this gives a complete protein in expression where the
accurate translation of the genetic message is an essential step in
gene expretion. The clone was found to encode an 202 amino-acid
protein fragment. It was expressed in Escherichia coli as a fusion
protein of calculated molecular mass of about 48 kDa with Cterminus
of glutathione-S-transferase ( about 26 kDa). The 202
amino-acid open reading frame encodes a protein with a calculated
molecular mass of about 22 kDa.

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