Article Abstract:
The IdiA protein from the cyanobacteria Synechococcus PCC 6301 was partially sequenced, indicating that the N-terminal amino acid is an alanine. Also, the gene encoding this protein has been identified and completely sequenced. The idiA gene codes for a protein starting with valine and consisting of 330 amino acid residues. Hence, IdiA seems to be synthesized as a precursor protein having an isoelectric point of 10.55. IdiA has similarities to two basic bacterial iron-binding proteins, SfuA from Serratia marcescens and Fbp from Neisseria gonorrhoeae.
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Article Abstract:
The cyanobacterium Synechococcus sp. strain PCC 7942 contains two alkaline phosphatases (APases) that are encoded by the phoV gene. These are the phosphate-repressible 145 kDa PhoA and the phosphate-irrepressible 61.3 kDa PhoV. The presence of a second APase is probably necessary to maintain the phosphate level in the cells under conditions of stress. Characterization of the gene product reveals that PhoV has a broad pH optimum, requires Zn2+ for activity and has a wide substrate specificity. Mn2+ and phosphate inhibit the protein.
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Article Abstract:
A study was conducted to analyze the characteristics of iron-deficiency-induced protein A (idiA) in Synechococcus PCC 6301 and the DNA region surrounding idiA in Synechococcus PCC 6301 and PCC 7942. Cyanobacteria were prepared in gas wash bottles. Experimental results indicated that the absence of two gene products prevents the elevated expression of idiA under nutrient deficiency.
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