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Updated: Jul 15, 2026

Generation of Marked and Markerless Mutants in Model Cyanobacterial Species
Published on: May 29, 2016
A novel covalent modification of nitrogenase in a cyanobacterium
J R Gallon1, J Cheng, L J Dougherty
1Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, UK. j.r.gallon@swansea.ac.uk
Abstract:
In extracts of the unicellular cyanobacterium Gloeothece, the Fe-protein of nitrogenase can be separated by SDS-PAGE into two antigenically identifiable components. Unlike the situation in photosynthetic bacteria such as Rhodospirillum rubrum, these two forms do not arise from covalent modification of the protein by ADP-ribosylation. Rather, the Fe-protein of Gloeothece nitrogenase is subjected to modification by palmitoylation.
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