Translation in vitro of rat brain messenger RNA coding for tubulin and actin.
A partially purified fraction of poly(a)-rich brain mRNA coding for tubulin and actin was obtained by stepwise elution from an oligo(deoxythymidylate)-cellulose column and was efficiently translated in a wheat-germ cell-free system. The newly synthesized tubulin and actin migrated along with the authentic proteins on sodium dodecyl sulfate polyacrylamide gels and on sodium dodecyl sulfate-urea polyacrylamide gels, where tubulin alpha- and beta-subunits are separated. The two proteins synthesized in vitro were found to be biologically active; they could be induced to polymerize and were both precipitated by vinblastine. In addition, specific binding of tubulin to an affinity column of colchicine-Sepharose and actin to myosin were demonstrated.
D000199:Actins / Q000096:biosynthesis*; D000818:Animals; D001921:Brain / Q000378:metabolism* / Q000648:ultrastructure; D002458:Cell Fractionation; D002474:Cell-Free System; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008870:Microtubules; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000096:biosynthesis*; D010944:Plants; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D051381:Rats; D014747:Vinblastine
D000199:Actins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D014747:Vinblastine