Molecular characterization and tissue-specific expression of the acetyl-CoA carboxylase α gene from Grass carp, Ctenopharyngodon idella

被引:32
作者
Cheng, Han-liang [1 ]
Ji, Nan-jing [1 ]
Peng, Yong-xing [1 ]
Shen, Xin [1 ]
Xu, Jian-he [1 ]
Dong, Zhi-guo [1 ]
Wu, Chen-chen [1 ]
机构
[1] Huaihai Inst Technol, Jiangsu Key Lab Marine Biotechnol, Lianyungang 222005, Jiangsu, Peoples R China
关键词
Grass carp; Acetyl-CoA Carboxylase; Full-length cDNA; Tissue expression; Real-time PCR; COENZYME-A CARBOXYLASE; PYRUVATE-CARBOXYLASE; 2; ISOFORMS; DOMAIN; SEQUENCE; CLONING; PHOSPHORYLATION; PREDICTION; MECHANISM; ENZYME;
D O I
10.1016/j.gene.2011.07.027
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Acetyl-CoA carboxylase alpha (ACC1), the major regulatory enzyme of fatty acid biosynthesis, catalyzes the conversion of acetyl-CoA to malonyl-CoA. The full-length cDNA coding ACC1 isoform was cloned from liver of grass carp. The cDNA obtained was 7515 bp with a 7173 bp open reading frame encoding 2389 amino acids. The ACC1 protein has a calculated molecular weight of 269.2 kDa and isoelectric point of 6.23. Tissue distribution of ACC1 mRNA in brain, mesenteric adipose, spleen, white muscle and liver of grass carp was analyzed by real-time PCR method using beta-actin as an internal control for cDNA normalization. The results showed that the expressions of ACC1 mRNA were detected in all examined tissues. Relative expression profile of ACC1 mRNA in liver normalized with beta-actin level was 15, 92, 135 and 165-fold compared with the level in brain, white muscle, mesenteric adipose and spleen, respectively. In addition, we present evidence for the presence of two isoforms of ACC1 (265.7 kDa and 267.2 kDa) in grass carp liver that differ from the 269.2 kDa ACC1 by the absence of 34 and 15 amino acids. In conclusion, the liver is one of the main ACC1 producing tissues in grass carp and ACC1 gene was highly homologous to that of mammals. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:46 / 51
页数:6
相关论文
共 25 条
[1]   HUMAN ACETYL-COA CARBOXYLASE - CHARACTERIZATION, MOLECULAR-CLONING, AND EVIDENCE FOR 2 ISOFORMS [J].
ABUELHEIGA, L ;
JAYAKUMAR, A ;
BALDINI, A ;
CHIRALA, SS ;
WAKIL, SJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (09) :4011-4015
[2]  
AbuElheiga L, 1997, J BIOL CHEM, V272, P10669
[3]   Goat acetyl-coenzyme A carboxylase α:: Molecular characterization, polymorphism, and association with milk traits [J].
Badaoui, B. ;
Serradilla, J. M. ;
Tomas, A. ;
Urrutia, B. ;
Ares, J. L. ;
Carrizosa, J. ;
Sanchez, A. ;
Jordana, J. ;
Amills, M. .
JOURNAL OF DAIRY SCIENCE, 2007, 90 (02) :1039-1043
[4]   ANALYSIS OF THE BIOTIN-BINDING SITE ON ACETYL-COA CARBOXYLASE FROM RAT [J].
BAI, DH ;
MOON, TW ;
LOPEZCASILLAS, F ;
ANDREWS, PC ;
KIM, KH .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 182 (02) :239-245
[5]   CLONING AND CHARACTERIZATION OF MULTIPLE ACETYL-COA CARBOXYLASE TRANSCRIPTS IN OVINE ADIPOSE-TISSUE [J].
BARBER, MC ;
TRAVERS, MT .
GENE, 1995, 154 (02) :271-275
[6]   Structure and regulation of acetyl-CoA carboxylase genes of metazoa [J].
Barber, MC ;
Price, NT ;
Travers, MT .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2005, 1733 (01) :1-28
[7]   Developmental regulation of alternatively spliced acetyl-CoA carboxylase-α mRNAs encoding isozymes with or without an eight amino acid domain upstream of the Ser-1200 phosphorylation motif in the mammary gland [J].
Barber, MC ;
Pooley, L ;
Travers, MT .
JOURNAL OF MOLECULAR ENDOCRINOLOGY, 2001, 27 (03) :349-356
[8]   Improved prediction of signal peptides: SignalP 3.0 [J].
Bendtsen, JD ;
Nielsen, H ;
von Heijne, G ;
Brunak, S .
JOURNAL OF MOLECULAR BIOLOGY, 2004, 340 (04) :783-795
[9]  
Dieffenbach CW., 1995, PCR PRIMER LAB MANUA
[10]   The biotin enzyme family: Conserved structural motifs and domain rearrangements [J].
Jitrapakdee, S ;
Wallace, JC .
CURRENT PROTEIN & PEPTIDE SCIENCE, 2003, 4 (03) :217-229