Identification of conserved promoter elements for aldB and isozyme specific residues in aldolase B

被引:7
作者
Berardini, TZ
Amsden, AB
Penhoet, EE
Tolan, DR
机构
[1] Boston Univ, Dept Biol, Boston, MA 02215 USA
[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1999年 / 122卷 / 01期
关键词
cis elements; DNA sequence; protein sequence; tissue-specific expression; introns; liver gene expression; protein structure; gene cloning;
D O I
10.1016/S0305-0491(98)10140-2
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
The comparison of three complete aldolase B genes-including known and putative regulatory elements-is presented. The third aldolase B gene was provided by the complete aldB gene sequence (14803 bp) encoding the rabbit aldolase B isozyme. The promoter sequence alignment included the nonmammalian chicken aldolase B gene and confirms the promoter sequence conservation of those elements where trans-factor binding has been demonstrated in rat aldB. Moreover, the alignment reveals conserved sequences that may represent previously unidentified promoter elements that are present in all aldBs or specifically in the mammalian aldB promoters. One remarkable feature is a poly-purine segment found between the CAAT and TATA elements. In the mammalian promoters, this is exclusively a 9-10 bp poly-dA stretch. The avian promoter has an additional stretch of eight dG-bases immediately upstream of the poly-dA. Alignment of a portion of intron 1 of the chicken, human, and rabbit aldB genes reveals conserved sequences that are likely candidates for a reported positive activation sequence. In addition, the amino acid sequences of all eight known aldolase B isozymes is compared to the other vertebrate aldolases. A. number of aldolase B-specific residues are identified that cluster in the carboxyl-portion of the sequence. With the exception of residue C268, these residues are not found near the active site, although, they are likely to be responsible for the substrate specificity of aldolase B. (C) 1999 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:53 / 61
页数:9
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