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Volume 270, Number 9, Issue of March 3, 1995 pp. 4624-4631
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Molecular Cloning and Sequencing of Arylphorin-binding Protein in Protein Granules of the Sarcophaga Fat Body
IMPLICATION OF A POST-TRANSLATIONAL PROCESSING MECHANISM

(Received for publication, August 15, 1994; and in revised form, November 29, 1994)

Sung Ook Chung,  Takeo Kubo ,  Shunji Natori

Previously, we identified an arylphorin-binding protein of Sarcophagaperegrina (flesh fly) with a molecular mass of 120 kDa and suggested its participation in the selective uptake of arylphorin from the hemolymph into the pupal fat body at metamorphosis (Ueno, K., and Natori, S.(1984) J. Biol. Chem. 259, 12107-12111). This paper reports the isolation and sequencing of cDNA for the 120-kDa protein. This protein consists of 1146 amino acid residues. Immunoblotting and RNA blotting experiments revealed that this protein is present as two fragments of 76 kDa (695 residues) and 53 kDa (451 residues) in the larval fat body. When larvae pupate, the 120-kDa protein gene is further activated and the complete 120-kDa protein is synthesized without fragmentation. This suggests a novel mechanism for the production of the 120-kDa protein regulated by a proteinase depending upon the stage of development of Sarcophaga. All of these proteins were found to be localized in protein granules in the adipocytes.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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