Literature DB >> 15310073

Characterization of RNase-like major storage protein from the ginseng root by proteomic approach.

Seung Il Kim1, Soo-Mi Kweon, Eun A Kim, Jin Young Kim, Soohyun Kim, Jong Shin Yoo, Young Mok Park.   

Abstract

The most abundant root proteins of ginseng (Panax ginseng) have been detected and identified by comparative proteome analysis with cultured hairy root of ginseng. Four abundant proteins (28, 26, 21 and 20 kDa) of P. ginseng had isoforms with different pl values on two-dimensional gel electrophoresis (2DE). The results of N-terminal and internal amino acid sequencing, however, showed that all of them originate from a 28 kDa protein, known as ginseng major protein (GMP). The GMP gene was searched for in the expressed sequence tag database of P. ginseng and found to encode a 27.3 kDa protein having 238 amino acid residues. Analysis of the amino acid sequences indicates that GMP exhibits high sequence homology with plant RNases and RNase-like proteins. However, purified GMP had no RNase activity even though it has conserved amino acid residues known to be essential for active sites of RNase. The GMPs present in ginseng main root were not expressed in cultured hairy roots of ginseng. 2DE analysis showed that the amounts of GMPs in main roots change according to seasonal fluctuation. These results suggest that the GMPs are root-specific RNase-like proteins, which function as vegetative storage proteins of ginseng for survival in the natural environment.

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Year:  2004        PMID: 15310073     DOI: 10.1016/j.jplph.2004.01.001

Source DB:  PubMed          Journal:  J Plant Physiol        ISSN: 0176-1617            Impact factor:   3.549


  9 in total

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