Abstract:
:The gene coding for the most abundant antifreeze protein (AFP) in the winter flounder was placed downstream of the Drosophila melanogaster hsp70 promoter and introduced into the D. melanogaster germ line by P-element-mediated transformation. In each of six transgenic strains tested, heat shock treatment induced the expression of two major AFP gene transcripts and one minor one. All three transcripts were spliced despite the lack of an obvious D. melanogaster internal intron-splicing sequence. The variation in transcript length was caused by selection of different polyadenylation sites. Western blots showed the presence of immunoreactive AFP in hemolymph from heat-shocked transformants. The immunoreactive material had a molecular weight of 6,200, which is consistent with the loss of the signal sequence from the primary translation product and the retention of the pro sequence. Thus, all the signals for flounder pre-mRNA and preprotein processing were recognized in D. melanogaster.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Rancourt DE,Walker VK,Davies PLdoi
10.1128/mcb.7.6.2188subject
Has Abstractpub_date
1987-06-01 00:00:00pages
2188-95issue
6eissn
0270-7306issn
1098-5549journal_volume
7pub_type
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