Molecular clone and sequence analysis of phenylalanine ammonia lyase gene from Camellia oleifera

doi:10.3969/j.jssn.1000-2006.2009.04.005

JOURNAL OF NANJING FORESTRY UNIVERSITY ›› 2009, Vol. 33 ›› Issue (04): 24-28.doi: 10.3969/j.jssn.1000-2006.2009.04.005

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Molecular clone and sequence analysis of phenylalanine ammonia lyase gene from Camellia oleifera

TIAN Xiaoming, TAN Xiaofeng*, HU Xiaoyi, LIU Qiao, LUO Qian

The Key Lab of Non Wood Forest Products of Forestry Ministry, Central South University of Forestry and Technology, Changsha 410004, China

Online:2009-08-18 Published:2009-08-18

Abstract

Abstract: PAL (phenylalanine ammonia lyase) is one of the key enzymes in plant secondary metabolism. The fulllength cDNA of PAL was identified from the cDNA library and EST library of Camellia oleifera by the method of molecular cloning in this paper. The results showed that the cDNA of C.oleifera PAL contained 2 118 bp, encoding 706 amino acids, and had a high similarity in the evolution of a high degree of homology with other species of PAL; C.oleifera PAL encoded protein sequence contained the same deamination site and catalytic active site with protein PAL of rice and corn. PAL phylogenetic tree analyses revealed that the C. oleifera PAL had closer relationship with PALs from Shrub plants than from other plants.

CLC Number:

Q785

TIAN Xiaoming, TAN Xiaofeng*, HU Xiaoyi, LIU Qiao, LUO Qian. Molecular clone and sequence analysis of phenylalanine ammonia lyase gene from Camellia oleifera[J]. JOURNAL OF NANJING FORESTRY UNIVERSITY, 2009, 33(04): 24-28.

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Molecular clone and sequence analysis of phenylalanine ammonia lyase gene from Camellia oleifera

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