Noncoordinate histone synthesis in heat-shocked Drosophila cells is regulated at multiple levels.
Transferring Drosophila tissue culture cells from 25 to 37 degrees C (heat shock) causes histone protein synthesis to become noncoordinate. To determine the level at which this is controlled, the synthesis, degradation, and translation of individual histone mRNAs was studied under both heat shock and control conditions. The increased synthesis of histone H2b protein during heat shock appears to be controlled primarily at the level of translation. During heat shock, H2b mRNA is transcribed at about the same level as in the control. However, H2b mRNA is more stable under heat shock than under control conditions and is predominantly found in polysomes. The reduction in synthesis of H2a, H3, and H4 protein during heat shock appears to be controlled at both the transcriptional and translational levels. Although transcription of H2a, H3, and H4 mRNAs is reduced during heat shock, like H2b mRNA, they are more stable. However, unlike H2b mRNA, these mRNAs are not predominantly associated with polysomes during heat shock. Regulation of H1 synthesis during heat shock is completely different from that of the other histones. During heat shock, H1 mRNA is not transcribed, and unlike all of the other Drosophila mRNAs studied to date, its mRNA is not stable in heat-shocked cells. Results from in vitro translation studies support the conclusion that noncoordinate synthesis of the core histone proteins during heat shock is controlled at the level of translation.
D000818:Animals; D046508:Culture Techniques; D004331:Drosophila melanogaster; D006657:Histones / Q000096:biosynthesis*; D006358:Hot Temperature; D011132:Polyribosomes / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D014158:Transcription, Genetic; D014544:Uridine Triphosphate / Q000378:metabolism
D006657:Histones; D012333:RNA, Messenger; D014544:Uridine Triphosphate