Disease relevance of Synpcc7942_0991

• The expression of a 126 kDa protein in the cytoplasmic membrane of Synechococcus PCC 7942 is shown to be dependent on the nitrogen source [1].
• Cyanobacteria possess thylakoid membranes that differ in their protein composition from the cytoplasmic membrane [2].
• We used antibodies raised against cytoplasmic membrane protein to find three genes with strong homology to sbpA, orf81 and cysT genes of the cyanobacterium Synechococcus sp. PCC 7942, Escherichia coli, Salmonella typhimurium and Marchantia polymorpha [3].
• This signal peptide-like sequence was capable of mediating protein translocation across the cytoplasmic membrane into the outer membrane of Escherichia coli, provided that this sequence was fused to the E. coli outer-membrane protein, OmpF [4].
• Different from Synechocystis sp. PCC 6803, where both respiration and ATP hydrolysis could be utilized for cytoplasmic membrane energization, proton extrusion at the cytoplasmic membrane in Synechococcus elongatus was preferentially driven by ATP hydrolysis [5].

High impact information on Synpcc7942_0991

• The three genes, cmpBCD, encode membrane components of an ATP-binding cassette transporter, whereas cmpA encodes a 42-kDa cytoplasmic membrane protein, which is 46.5% identical to the membrane-anchored substrate-binding protein of the nitrate/nitrite transporter [6].
• Cyanobacteria possess thylakoid membranes that differ in their protein composition from the cytoplasmic membrane [7].
• DNA sequence and regulation of the gene (cbpA) encoding the 42-kilodalton cytoplasmic membrane carotenoprotein of the cyanobacterium Synechococcus sp. strain PCC 7942 [8].
• The initial rate of sulfate uptake increased between 2 and 6 h after transfer of the cells to sulfur-free medium, in concert with elevated levels of three cytoplasmic membrane polypeptides with molecular masses of 43, 42, and 36 kilodaltons (kDa) [9].
• Localization of Slr1295 provided evidence that it has an intracellular function, since virtually no Slr1295 was detected in the soluble protein fraction of the periplasm or in the cytoplasmic membrane [10].

Chemical compound and disease context of Synpcc7942_0991

• These results may suggest involvement of the 126 kDa protein in nitrate transport through Synechococcus cytoplasmic membrane [1].
• Most cyanobacteria take up nitrate or nitrite through a multisubunit ABC transporter (ATP-binding cassette) located in the cytoplasmic membrane [11].

Biological context of Synpcc7942_0991

• Na+ influx under dark aerobic conditions occurred independently of delta pH or delta psi across the cytoplasmic membrane, ATPase activity, and respiratory electron transport [12].

Associations of Synpcc7942_0991 with chemical compounds

• A thermotrophic phase transition of lipids within the cytoplasmic membrane of intact cells was also revealed by detecting the temperature-dependent absorption changes in the proportion of zeaxanthin at 390 nm [13].
• Acridine yellow and Acridine orange proved to be the best DeltapH indicators for the investigation of thylakoid and cytoplasmic membrane energization: While Acridine yellow indicated only cytosolic energization, Acridine orange showed signals from both the thylakoid lumen and the cytosol that could be separated kinetically [5].

Other interactions of Synpcc7942_0991

• The secY gene product is an essential component of the Escherichia coli cytoplasmic membrane, which mediates the protein translocation across the membrane [14].

Analytical, diagnostic and therapeutic context of Synpcc7942_0991

• The protein has been localized in the cytoplasmic membrane by biochemical procedures as well as by electron microscopic immunocytochemistry [8].

References