The subunit composition of cerebellar tubulin: evidence for multiple beta tubulin messenger RNAs.
Cytoplasmic proteins were isolated from adult rat forebrain and cerebellum and analyzed by two-dimensional gel electrophoresis under conditions which the major subunits of tubulin were separated. Forebrain cytoplasmic tubulin consisted of two groups of alpha subunits (alpha 1 and alpha 2) and a minimum of two beta subunits (beta 1 and beta 2). However, the rat cerebellar cytoplasmic proteins contained greatly decreased amounts of the beta 1 tubulin subunit relative to the analysis of forebrain proteins. Messenger RNA (mRNA) was purified from cerebellum and forebrain and translated in wheat germ homogenate. Analysis of the translation products of cerebellar mRNA indicated only a trace amount of the beta 1 subunit, whereas the expected amount of beta 1 was found among the translation products of forebrain mRNA. This data is consistent with the conclusion that the beta 1 and beta 2 subunits of tubulin are synthesized from different mRNAs. A decrease in beta 1 mRNA relative to other tubulin mRNAs may be one of the factors responsible for the low steady state amounts of beta 1 tubulin in the cerebellum.
D000818:Animals; D001921:Brain / Q000378:metabolism; D002531:Cerebellum / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins / Q000096:biosynthesis; D012333:RNA, Messenger / Q000235:genetics*; D051381:Rats; D014404:Tubulin / Q000096:biosynthesis / Q000235:genetics*
D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D014404:Tubulin