Sequencing and Modification of the Gene Encoding the 42-Kilodalton Protein in the Cytoplasmic Membrane of Synechococcus PCC 7942
Author(s) -
Tatsuo Omata,
Thomas J. Carlson,
Teruo Ogawa,
J. Rush Pierce
Publication year - 1990
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.93.1.305
Subject(s) - kilodalton , synechococcus , mutant , cytoplasm , biology , mutagenesis , gene , biochemistry , microbiology and biotechnology , transformation (genetics) , insertional mutagenesis , cyanobacteria , genetics , bacteria
A 42-kilodalton cytoplasmic membrane protein is synthesized when high CO(2)-grown cells of Synechococcus PCC 7942 (Anacystis nidulans R2) are exposed to low CO(2). The structural gene for this protein (cmpA) has been cloned and sequenced and shown to encode a 450 amino acid polypeptide with a molecular mass of 49 kilodalton. A deletion mutant lacking the 42-kilodalton protein was obtained by transformation of Synechococcus PCC 7942 following in vitro mutagenesis of the cloned gene. There were no significant differences between the mutant and wild-type cells in their growth rates under either low or high CO(2) conditions. The activity of inorganic carbon (C(i)) transport in the mutant was as high as that in the wild-type strain. In both types of cells, CO(2) was the main species of C(i) transported and the activities of CO(2) and HCO(3) (-) transport increased when high CO(2)-grown cells were exposed to low CO(2). We conclude that the 42-kilodalton protein is not directly involved in the C(i)-accumulating mechanism of Synechococcus PCC 7942.
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