Molec. gen. Genet. 159, 85-87 (1978)
© by Springer-Verlag 1978
lmaginal Disc Ribosomal Proteins of D. melanogaster*
lffva Fekete
Institute of Genetics, Biological Research Center of the Hungarian Academy of Sciences, P.O.B. 521, H-6701 Szeged, Hungary
Andrew G. Lambertsson**
Department of Genetics, University of Ume~, S-90187 Umegt, Sweden
Summary. The ribosomal proteins from undifferen-
tiated imaginal discs of Drosophila melanogaster were
analyzed by two-dimensional gel electrophoresis and
compared with the ribosomal protein pattern of adult
flies. It is shown that the ribosomal proteins from
these discs are qualitatively identical with those of
adult flies except that two acidic proteins are missing
in the discs. This heterogeneity is discussed in terms
of the functional roles these two proteins may carry
in connection with disc differentiation.
Introduction
An important and characteristic feature of the devel-
opment of holometabolous insects such as Drosophila
is the establishment, within one individual, of two
systems, a larval and an imaginal one. The former
(the epidermis, the salivary glands, the fat bodies,
the intestine, and the muscles) is programmed to de-
generate, and the latter (the imaginal discs) to un-
dergo rapid and extensive differentiation, forming the
adult structures. The imaginal discs are derived from
the epidermis during embryogenesis and are not of
vital importance before the pupal stage. The number
of cells in the discs remains stationary during embryo-
genesis, but then increases continuously and exponen-
tially throughout the larval period (N6thiger, 1972).
Under the influence of ecdysone, the steroid insect
molting hormone, the discs undergo morphogenesis.
The initial phase of this process is termed evagination
and is dependent on continued protein synthesis (Fris-
trom et al., 1973).
Previous studies, using whole animals, disclosed
qualitative changes in the protein composition of Dro-
* Paper No. 6 of the present series. Paper No. 5 is by Lamberts-
son, A.G. Molec. gen. Genet. 139, 145-156 (1975)
** To whom all correspondence should be sent
sophila ribosomes during development (Lambertsson
et al., 1970; Lambertsson, 1972, 1974), the alterations
taking place during the third larval instar (Lamberts-
son, 1975). In view of these findings, and the observa-
tion that the cells of mature discs are packed full
with free ribosomes (Ursprung, 1972), it was of inter-
est to know the ribosomal protein composition of
undifferentiated imaginal discs. The results presented
in this paper demonstrate that the ribosomal proteins
of imaginal discs and adult flies are qualitatively
identical except that two acidic proteins are missing
in the discs,
Material and Methods
The Preparative Isolation of Imaginal Discs. Imaginal discs were
isolated from the Oregon R wild-type strain according to the pre-
parative procedure described by Fristrom (1972). The imaginal
disc fraction was estimated to have a purity of 90-95%. The discs
were frozen and stored at -30 ° C until used.
Preparation of Ribosomes and Ribosomal Proteins. The conditions
for the preparation of high salt-washed ribosomes were the same
as described before (Lambertsson, 1974) with the following modifi-
cations: a) imaginaI discs (1 1.5 g, wet weight) were homogenized
in 5 ml of buffer A (0.25 M sucrose, 0.05 M Tris-HCl, pH 7.6, 0.01 M
MgCI2, 0.05 M NH,C1, 0.01 M mercaptoethanol, and 1% Triton
X-100), using a Dounce all-glass homogenizer, and b) 4 ml of
the mitochondria-free supematant was underlayed with 1 ml of
buffer B (1.0 M sucrose, 0.05 M Tris-HC1, pH 7.6, 0.01 M MgC12,
0.50 M NH4CI, and 0.02 M mercaptoethanol), and the ribosomes
were pelleted by ultracentrifugation for 4 h at 160000 x g.
The ribosomal proteins were extracted with 67% acetic acid
in the presence of 33 mM Mg~ + (Hardy et al., 1969; Lambertsson,
1975). The proteins were precipitated with 9 volumes of cold ace-
tone, washed twice with acetone, and dried in vaeuo (Lambertsson
et al., 1970).
Two-Dimensional Electrophoresis. Two-dimensional polyacryl-
amide gel electrophoresis was performed as previously described
(Lambertsson, 1975), except that the 2-D apparatus was modified
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