EXPRESSION OF RAT-LIVER ADOHCY HYDROLASE IN A RHODOBACTER-CAPSULATUS AHCY MUTANT RESTORES PIGMENT FORMATION AND PHOTOSYNTHETIC GROWTH

被引：3

作者：

AKSAMIT, RR ^{[1
]}

BUGGY, JJ ^{[1
]}

BAUER, CE ^{[1
]}

机构：

[1] INDIANA UNIV, DEPT BIOL, BLOOMINGTON, IN 47405 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 207卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.1182

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：

An amino acid alignment of fourteen S-adenosylhomocysteine hydrolases shows that sequences from six photosynthetic species and one species possibly derived from algae have an internal 36 to 41 amino acid sequence that is not present in hydrolase sequences from seven nonphotosynthetic species. In the photosynthetic eubacterium Rhodobacter capsulatus, the StLB1 strain has a disrupted hydrolase gene, and hydrolase activity is not detectable. Photopigment synthesis and photosynthetic growth are significantly reduced in the StLB1 strain. Introduction of rat hydrolase cDNA into the StLB1 strain restored hydrolase activity, photopigment synthesis and photosynthetic growth. The results show that the 36 amino acid sequence of Rhodobacter capsulatus S-adenosylhomocysteine hydrolase does not have a photosynthesis specific function. (C) 1995 Academic Press, Inc..

引用

页码：265 / 272

页数：8

共 28 条

[1]

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[2]

BAUER CE, 1988, J BIOL CHEM, V263, P4820

[3] SEQUENCE OF FULL LENGTH CDNA FOR HUMAN S-ADENOSYLHOMOCYSTEINE HYDROLASE [J].