Cloning and characterization of the ddsA gene encoding decaprenyl diphosphate synthase from Rhodobacter capsulatus B10

被引：3

作者：

Liu, Xinyi ^{[1
]}

Wu, Haizhen ^{[1
]}

Ye, Jiang ^{[1
]}

Yuan, Oinsheng ^{[1
]}

Zhang, Huizhan ^{[1
]}

机构：

[1] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

来源：

CANADIAN JOURNAL OF MICROBIOLOGY | 2006年 / 52卷 / 12期

关键词：

ubiquinone; polyprenyl diphosphate synthase; gene expression; Rhodobacter capsulatus;

D O I：

10.1139/W06-080

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 decaprenyl diphosphate synthase gene (ddsA, GenBank accession No. DQ191802) was cloned from Rhodobacter capsulatus 1310 by constructing and screening the genome library. An open reading frame of 1002 bp was revealed from sequence analysis. The deduced polypeptide consisted of 333 amino acids residues with an molecular mass of about 37 kDa. The DdsA protein contained the conserved amino acid sequence (DDXXD) of E-type polyprenyl diphosphate synthase and showed high similarity to others. In contrast, DdsA showed only 39% identity to a solanesyl diphosphate synthase cloned from R. capsulatus SB1003. DdsA was expressed successfully in Escherichia coli. Assaying the enzyme in vivo found it made E.coli synthesize UQ-10 in addition to the endogenous production UQ-8.

引用

页码：1141 / 1147

页数：7

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