A novel covalent modification of nitrogenase in a cyanobacterium.
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.
Gallon
J R
JR
Biochemistry Research Group, School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea, UK. j.r.gallon@swansea.ac.uk
Cheng
J
J
Dougherty
L J
LJ
Gallon
V A
VA
Hilz
H
H
Pederson
D M
DM
Richards
H M
HM
Rüggeberg
S
S
Smith
C J
CJ
D000458:Cyanobacteria / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D008667:Metalloproteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D009591:Nitrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D019308:Palmitic Acid / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D008667:Metalloproteins; D019308:Palmitic Acid; D009591:Nitrogenase