Isolation and characterization of the Drosophila melanogaster gene encoding translation-initiation factor eIF-2 beta.
Drosophila melanogaster cDNA clones encoding the beta subunit of translation initiation factor 2 (eIF-2) were isolated and sequenced. The longest cDNA predicts a protein of 312 amino acids (aa), which possesses a putative RNA-binding motif and a highly charged N-terminal region composed of three basic polylysine blocks. The aa sequence comparison of D. melanogaster eIF-2 beta with its human and yeast counterparts demonstrates a high degree of similarity, especially within the C-terminal region. Northern analysis indicates quasi-constitutive expression of eIF-2 beta throughout D. melanogaster development.
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Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235.
Cavener
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004331:Drosophila melanogaster / Q000196:embryology / Q000235:genetics*; D015852:Eukaryotic Initiation Factor-2 / Q000737:chemistry / Q000235:genetics*; D005260:Female; D017344:Genes, Insect / Q000235:genetics*; D006801:Humans; D007814:Larva / Q000737:chemistry; D008297:Male; D008969:Molecular Sequence Data; D011679:Pupa / Q000737:chemistry; D012333:RNA, Messenger / Q000032:analysis; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D016335:Zinc Fingers / Q000235:genetics
D018076:DNA, Complementary; D015852:Eukaryotic Initiation Factor-2; D012333:RNA, Messenger