Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis.
The rate of protein synthesis in metaphase-arrested cells is reduced as compared to interphase cells. The reduction occurs at the translation initiation step. Here, we show that, whereas poliovirus RNA translation is not affected by the mitotic translational block, the translation of vesicular stomatitis virus mRNAs is. In an attempt to elucidate the mechanism by which initiation of protein synthesis is reduced in mitotic cells, we found that the interaction of the mRNA 24-kDa cap-binding protein (CBP) with the mRNA 5' cap structure is reduced in mitotic cell extracts, consistent with their lower translational efficiency. Addition of cap-binding protein complex stimulated the translation of endogenous mRNA in extracts from mitotic but not interphase cells. In addition, we found that the 24-kDa CBP from mitotic cells was metabolically labeled with 32P to a lesser extent than the protein purified from interphase cells. These results are consistent with a hypothesis that the 24-kDa CBP is implicated in the inhibition of protein synthesis in metaphase-arrested cells. Possible mechanisms for this inhibition are offered.
D016590:Aphidicolin; D004224:Diterpenes / Q000494:pharmacology; D039562:Eukaryotic Initiation Factor-4F; D006367:HeLa Cells / Q000378:metabolism / Q000382:microbiology; D006801:Humans; D007399:Interphase; D008938:Mitosis; D010448:Peptide Initiation Factors / Q000378:metabolism*; D010766:Phosphorylation; D017955:Poliovirus / Q000235:genetics; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics
D004224:Diterpenes; D039562:Eukaryotic Initiation Factor-4F; D010448:Peptide Initiation Factors; D012333:RNA, Messenger; D012367:RNA, Viral; D016590:Aphidicolin