The light harvesting chlorophyll a/b-binding protein is one of key proteins in the transformation from light energy to chemical energy. An open reading frame coding precursor protein of cab gene was cloned from the fi...The light harvesting chlorophyll a/b-binding protein is one of key proteins in the transformation from light energy to chemical energy. An open reading frame coding precursor protein of cab gene was cloned from the first strand of bamboo cDNA through RT-PCR methods,and named as cab-PhE1 (cab gene 1 from Phyllostachys edulis EF207229). The sequence analysis showed that the deduced polypeptide was highly homologous to some other CAB proteins from monocotyledon,and the gene belonged to lhcb2 family. Tissue specific expression showed that cab-PhE1 expressed higher in leaf than sheath and stem. The prokaryotic expression vector of cab-PhE1 gene encoding the mature protein was constructed by subcloning the fragment into pET-23 a and was expressed in Escherichia coli induced by IPTG. The molecular weight of the induced protein was about 28 ku,approximate to that of the mature protein. This work is a key to the further research on in vitro reconstitution of light-harvesting Chl a/b complexes.展开更多
As a critical enzyme in secondary metabolism of plant,Phenylanlanine ammonialyase(PAL) has significant meaning to its development and strong tolerance ability against hard.A full-length cDNA of PAL gene was isolated f...As a critical enzyme in secondary metabolism of plant,Phenylanlanine ammonialyase(PAL) has significant meaning to its development and strong tolerance ability against hard.A full-length cDNA of PAL gene was isolated from Phyllostachys edulis through RT-PCR and RACE methods,and named as PePAL1(GenBank accession number:FJ195650).PePAL1 is 2 436 bp,which contains an open reading frame encoding 701 amino acids.The results of amino acid sequence analysis showed that PePAL1 had high identities with other gramineous PAL in Oryza sativa,Zea mays,Saccharum officinarum,Bambusa ventricosa,Bambusa oldhamii and Triticum aestivum,especially with PAL from O.sativa up to 93.0%.Phylogenetic analysis showed that PePAL1 and LLB1 were on different branch sites.Tissue specific expression showed that PePAL1 expressed in leaf,sheath,stem and root,much higher in stem.展开更多
文摘The light harvesting chlorophyll a/b-binding protein is one of key proteins in the transformation from light energy to chemical energy. An open reading frame coding precursor protein of cab gene was cloned from the first strand of bamboo cDNA through RT-PCR methods,and named as cab-PhE1 (cab gene 1 from Phyllostachys edulis EF207229). The sequence analysis showed that the deduced polypeptide was highly homologous to some other CAB proteins from monocotyledon,and the gene belonged to lhcb2 family. Tissue specific expression showed that cab-PhE1 expressed higher in leaf than sheath and stem. The prokaryotic expression vector of cab-PhE1 gene encoding the mature protein was constructed by subcloning the fragment into pET-23 a and was expressed in Escherichia coli induced by IPTG. The molecular weight of the induced protein was about 28 ku,approximate to that of the mature protein. This work is a key to the further research on in vitro reconstitution of light-harvesting Chl a/b complexes.
文摘As a critical enzyme in secondary metabolism of plant,Phenylanlanine ammonialyase(PAL) has significant meaning to its development and strong tolerance ability against hard.A full-length cDNA of PAL gene was isolated from Phyllostachys edulis through RT-PCR and RACE methods,and named as PePAL1(GenBank accession number:FJ195650).PePAL1 is 2 436 bp,which contains an open reading frame encoding 701 amino acids.The results of amino acid sequence analysis showed that PePAL1 had high identities with other gramineous PAL in Oryza sativa,Zea mays,Saccharum officinarum,Bambusa ventricosa,Bambusa oldhamii and Triticum aestivum,especially with PAL from O.sativa up to 93.0%.Phylogenetic analysis showed that PePAL1 and LLB1 were on different branch sites.Tissue specific expression showed that PePAL1 expressed in leaf,sheath,stem and root,much higher in stem.
