Molecular characterization of a phosphoserine aminotransferase gene in Antheraea pernyi and assessment of its value for phylogenetic inference

被引:4
作者
Wang, Zhen-Dong [1 ]
Jiang, Yi-Ren [1 ]
Sun, Ying [1 ]
Li, Qun [1 ]
Li, Yu-Ping [1 ]
Du, Zhan-Jun [2 ]
Liu, Yan-Qun [1 ,2 ]
Qin, Li [1 ]
机构
[1] Shenyang Agr Univ, Insect Resource Ctr Engn & Technol Liaoning Prov, Shenyang 110866, Peoples R China
[2] Sericultural Inst Liaoning Prov, Key Lab Wild Silkmoth Res Liaoning Prov, Fengcheng 118110, Peoples R China
关键词
Antheraea pernyi; Phosphoserine aminotransferase; Expression pattern; Phylogenetic inference; CHINESE OAK SILKWORM; SERINE BIOSYNTHESIS; EXPRESSION PATTERN; PHOSPHORYLATED PATHWAY; ESCHERICHIA-COLI; CLONING; EVOLUTION; HOMOLOGY; PROTEIN; METABOLISM;
D O I
10.1016/j.bse.2013.01.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A gene encoding phosphoserine aminotransferase from Antheraea pernyi (ApPSAT) was isolated and characterized, and its value for phylogenetic inference was assessed. The resulting 1309 bp cDNA sequence contains an open reading frame of 1095 bp encoding a polypeptide of 364 amino acids, with 58% sequence identity to that from Homo sapiens. RTPCR analysis showed that the ApPSAT gene was transcribed at four developmental stages, and in all examined tissues with the most abundance in malpighian tubules. Sequence alignment suggested that ApPSAT protein sequence exhibited 41-87% homology with the known PSATs from bacteria, fungi, plants, invertebrates and vertebrates. Phylogenetic analysis revealed that 37 representative PSAT protein sequences were well divided into five groups corresponding to the known fungi, bacteria, plants, invertebrates and vertebrates. The phylogenetic relationships obtained were consistent with the traditional classification and other molecular data, suggesting the potential value of the PSAT protein in phylogenetic inference. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:293 / 300
页数:8
相关论文
共 34 条
[1]   Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway Of L-serine biosynthesis [J].
Baek, JY ;
Jun, DY ;
Taub, D ;
Kim, YH .
BIOCHEMICAL JOURNAL, 2003, 373 :191-200
[2]   The PROSITE database, its status in 1995 [J].
Bairoch, A ;
Bucher, P ;
Hofmann, K .
NUCLEIC ACIDS RESEARCH, 1996, 24 (01) :189-196
[3]   A GENE FROM SACCHAROMYCES-CEREVISIAE WHICH CODES FOR A PROTEIN WITH SIGNIFICANT HOMOLOGY TO THE BACTERIAL 3-PHOSPHOSERINE AMINOTRANSFERASE [J].
BELHUMEUR, P ;
FORTIN, N ;
CLARK, MW .
YEAST, 1994, 10 (03) :385-389
[4]   SilkDB v2.0: a platform for silkworm (Bombyx mori) genome biology [J].
Duan, Jun ;
Li, Ruiqiang ;
Cheng, Daojun ;
Fan, Wei ;
Zha, Xingfu ;
Cheng, Tingcai ;
Wu, Yuqian ;
Wang, Jun ;
Mita, Kazuei ;
Xiang, Zhonghuai ;
Xia, Qingyou .
NUCLEIC ACIDS RESEARCH, 2010, 38 :D453-D456
[5]  
[葛君 Ge Jun], 2010, [蚕业科学, Acta Sericologica Sinica], V36, P428
[6]   Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 Å resolution:: Comparison of the unligated enzyme and a complex with α-methyl-L-glutamate [J].
Hester, G ;
Stark, W ;
Moser, M ;
Kallen, J ;
Markovic-Housley, Z ;
Jansonius, JN .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 286 (03) :829-850
[7]   Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis from Arabidopsis [J].
Ho, CL ;
Noji, M ;
Saito, M ;
Yamazaki, M ;
Saito, K .
PLANT JOURNAL, 1998, 16 (04) :443-452
[8]   Molecular cloning of ribosomal protein L26 (RPL26) cDNA from Ailuropoda melanoleuca and its potential value in phylogenetic study [J].
Hon, Wan-ru ;
Sun, Genlou ;
Chen, Yu ;
Wu, Xia ;
Peng, Zheng-Song ;
Zhou, Caiquan .
BIOCHEMICAL SYSTEMATICS AND ECOLOGY, 2008, 36 (03) :194-200
[9]   Structure, evolution and action of vitamin B6-dependent enzymes [J].
Jansonius, JN .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1998, 8 (06) :759-769
[10]  
Li YP, 2009, INT J BIOL SCI, V5, P451