A novel covalent modification of nitrogenase in a cyanobacterium

• Published in: FEBS letters Vol. 468; no. 2; pp. 231 - 233
• Main Authors: Gallon, John R., Cheng, Jiujun, Dougherty, Lisa J., Gallon, Victoria A., Hilz, Helmuth, Pederson, Dennis M., Richards, Helen M., Rüggeberg, Sabrina, Smith, Christopher J.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 25.02.2000
• Subjects: Covalent modification; Cyanobacteria - enzymology; Cyanobacterium; Electrophoresis, Polyacrylamide Gel; Fe-protein; Gloeothece; HEPES, N-2-hydroxyethylpiperazine-N′-2-ethanesulphonic acid; HPTLC, high performance thin layer chromatography; MALDI, matrix-assisted laser desorption; Metalloproteins - chemistry; Metalloproteins - isolation & purification; Metalloproteins - metabolism; Nitrogenase; Nitrogenase - chemistry; Nitrogenase - isolation & purification; Nitrogenase - metabolism; PAGE, polyacrylamide gel electrophoresis; Palmitic Acid - metabolism; Palmitoylation; PPO, 2,5-diphenyloxazole; Protein Processing, Post-Translational; TOF, time of flight; MALDI, matrix-assisted laser desorption; TOF, time of flight; Cyanobacterium; HPTLC, high performance thin layer chromatography; Covalent modification; Palmitoylation; PAGE, polyacrylamide gel electrophoresis; Nitrogenase; HEPES, N-2-hydroxyethylpiperazine- N′-2-ethanesulphonic acid; Fe-protein; PPO, 2,5-diphenyloxazole; Gloeothece
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(00)01229-1

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.