TY - JOUR
T1 - Preferential expression of actin genes during oogenesis of Drosophila
AU - Ruddell, Alanna
AU - Jacobs-Lorena, Marcelo
N1 - Funding Information:
We thank Dr. E. Fyrberg for kindly providing the cloned actin probes. We also thank Drs. J. Ilan, A. Mahowald, D. Samols, and M. Kay for helpful comments on the manuscript. This investigation was supported by NIH Grants GM 25327 and GM 07225.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1984/9
Y1 - 1984/9
N2 - The expression of actin genes was examined during oogenesis of Drosophila. Accumulation of actin proteins was quantitated by a two-stage electrophoresis procedure. Egg chambers accumulate actins preferentially, resulting in a twofold enrichment over other nonyolk proteins. RNA gel blot hybridization experiments demonstrated a concomitant twofold selective increase of actin mRNA levels over that of other mRNAs, suggesting regulation of actin genes at the pretranslational level. Despite an abrupt arrest of actin protein accumulation near the end of oogenesis, the bulk of the actin mRNAs remains associated with polysomes of constant size. It appears that this shut-off of actin protein accumulation is due to an overall decrease in translational efficiency, rather than actin mRNA degradation or its dissociation from polysomes.
AB - The expression of actin genes was examined during oogenesis of Drosophila. Accumulation of actin proteins was quantitated by a two-stage electrophoresis procedure. Egg chambers accumulate actins preferentially, resulting in a twofold enrichment over other nonyolk proteins. RNA gel blot hybridization experiments demonstrated a concomitant twofold selective increase of actin mRNA levels over that of other mRNAs, suggesting regulation of actin genes at the pretranslational level. Despite an abrupt arrest of actin protein accumulation near the end of oogenesis, the bulk of the actin mRNAs remains associated with polysomes of constant size. It appears that this shut-off of actin protein accumulation is due to an overall decrease in translational efficiency, rather than actin mRNA degradation or its dissociation from polysomes.
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U2 - 10.1016/0012-1606(84)90266-5
DO - 10.1016/0012-1606(84)90266-5
M3 - Article
C2 - 6205919
AN - SCOPUS:0021485569
VL - 105
SP - 115
EP - 120
JO - Developmental Biology
JF - Developmental Biology
SN - 0012-1606
IS - 1
ER -