Biochemical evidence for the presence of an unconventional actin protein in a prokaryotic organism.
The ubiquity of actin, like the functional diversity of many associated proteins, raises a question concerning diversification of motility mechanisms and thus the emergence of an elementary functional system. Our aim was to investigate, in particular, mobiles prokaryotics cells as Synechocystis lacking cilia and flagella, search for actin essential properties and then locate the molecular behaviours. Here we report the presence and purification of a 56-kDa (apparent molecular weight) prokaryotic protein that polymerizes to form filaments, activates myosin Mg(++)-ATPase activity, inhibits DNase-1 activity and affords close antigenic homology to skeletal actin. This protein was found to be associated with thylakoid membranes and extracted in the presence of Triton X-100.
Labbé
J P
JP
Centre de Recherches de Biochimie Macromoleculaire UPR 8402 (CNRS), U 249 (INSERM), Université de Montpellier, France.
Harricane
M C
MC
Boyer
M
M
Derancourt
J
J
Roustan
C
C
Benyamin
Y
Y
D000199:Actins / Q000502:physiology*; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*; D002465:Cell Movement / Q000502:physiology; D000458:Cyanobacteria / Q000737:chemistry*; D003850:Deoxyribonuclease I / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D018482:Muscle, Skeletal / Q000737:chemistry; D009218:Myosins / Q000378:metabolism; D011108:Polymers; D011817:Rabbits
D000199:Actins; D001426:Bacterial Proteins; D011108:Polymers; D003850:Deoxyribonuclease I; D009218:Myosins