Comparison of the consensus sequence flanking translational start sites in<i>Drosophila</i>and vertebrates

Cavener, Douglas R.

doi:10.1093/nar/15.4.1353

Cited by 974 publications

(514 citation statements)

References 38 publications

Supporting

Mentioning

473

Contrasting

Unclassified

Order By: Relevance

“…Both of these predicted M,.s are in close agreement with the apparent M, (i.e., 55 000) of the monomeric unit of G6PD (Lee et al, 1978;Williamson and Bentley, 1983). Examination of the 5' sequences flanking the two potential translation start sites shows that neither strongly match the generalized Drosophila initiation consensus sequence proposed by Cavener (1987) (Table I). However, a comparison of these 5' sequences with those sequences 5' of the translational start sites of 83 other Drosophila genes reveals that the sequence 5' of the first ATG is very similar to those of the glue protein Sgs4 while those 5' of the second ATG are similar to Hsp-22 (Table 1).…”

Section: (D) Identification Of the Protein Coding Regionmentioning

confidence: 82%

Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene

Fouts

Ganguly

Gutierrez

et al. 1988

Gene

View full text Add to dashboard Cite

Section: (D) Identification Of the Protein Coding Regionmentioning

confidence: 82%

Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene

Fouts

Ganguly

Gutierrez

et al. 1988

Gene

View full text Add to dashboard Cite

“…The 2.2-kb cDNA contains an open reading frame of 465 amino acids. The sequence surrounding the ®rst ATG is in good match with the Drosophila consensus for translational initiation (Cavener, 1987). The DAP-2 initiation and termination codons and the polyadenylation signal sequence are printed in bold letters.…”

Section: Cloning Of Drosophila Ap-2mentioning

confidence: 99%

“…Triangles represent splice sites in hAP-2a (!) and DAP-2 (~) the Drosophila consensus sequence¯anking the translational start site (Cavener, 1987). The ®rst inframe stop codon is found at position 1806, and the ®rst polyadenylation signal at position 1887.…”

Section: Cloning Of Drosophila Ap-2mentioning

confidence: 99%

Cloning and characterization of the Drosophila homologue of the AP-2 transcription factor

et al. 1998

View full text Add to dashboard Cite

The AP-2 family of transcription factors (AP-2a, AP-2b and AP-2g) is temporally and spatially regulated in mammals and has also been implicated in oncogenesis. Here we report the isolation of genomic and cDNA clones encoding the Drosophila homologue of AP-2, designated DAP-2. The predicted amino acid sequence exhibits 42 ± 45% overall identity with the vertebrate AP-2 proteins. A sequence of 107 amino acids within the DNA binding and dimerization domain of the vertebrate AP-2 proteins is highly conserved (90 ± 92%) with the DAP-2 homologue. An in vitro translation product of DAP-2 cDNA binds speci®cally to AP-2 consensus binding sites. DAP-2 was also shown to be functionally conserved in vivo because transient transfection of a DAP-2 expression plasmid activated transcription through AP-2 binding sites in both mammalian and Drosophila cell lines. DAP-2 is expressed during early embryogenesis and DAP-2 transcripts are also detected in the adult. Whole-mount in situ hybridizations demonstrated that DAP-2 is expressed initially at stage 9 of Drosophila embryonic development and that DAP-2 transcripts are detected in regions of the brain, eyeantennal disc, optical lobe, antenno-maxillary complex, and in a subset of cells of the ventral nerve cord. The cloning of DAP-2 and the identi®cation of the DAP-2 expression pattern during embryogenesis provides a starting point to address the function of AP-2 during di erentiation and development in a well understood model system.

show abstract

“…The open reading frame was anked by 314 nt and 842 nt 5' and 3' untranslated sequences, respectively. The putative translational initiation codon matched the Drosophila translational initiator consensus sequence (Cavener, 1987) including a purine at the 73 position. A second in frame ATG occurred 186 nt 3' that also corresponded to a favourable translational consensus sequence.…”

Section: Isolation Of a Drosophila Gene With Similarity To C-cblmentioning

confidence: 99%

D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites

Hime

Dhungat

et al. 1997

Oncogene

View full text Add to dashboard Cite

The c-Cbl proto-oncogene encodes a multidomain phosphoprotein that has been demonstrated to interact with a wide range of signalling proteins. The biochemical function of c-Cbl in these complexes is, however, unclear. Recent studies with the C. elegans Cbl homologue, sli-1, have suggested that Cbl proteins may act as negative regulators of EGF receptor (EGFR) signalling. As the EGFR and other protein tyrosine kinase receptor signalling pathways are highly conserved between insects and vertebrates, we sought a Drosophila homologue of cCbl for a detailed genetic analysis. We report here that Drosophila melanogaster has a single gene, D-cbl, that is homologous to c-cbl. We ®nd that D-cbl encodes a 52 kDa protein that has a high degree of similarity to cCbl and SLI-1 across novel phosphotyrosine-binding (PTB) and RING ®nger domains. Surprisingly, however, D-Cbl is C-terminally truncated relative to c-Cbl and SLI-1 and consequently is unable to bind SH3-domain containing adaptor proteins, including the Drosophila Grb2 homologue, Drk. Although the D-Cbl protein lacks Drk binding sites it can nevertheless associate with a tyrosine phosphorylated protein, or is itself tyrosine phosphorylated in an DER dependent manner and associates with activated Drosophila EGF receptors (DER) in vivo. Consistent with a role for D-Cbl in DER dependent patterning in the embryo and adult, DCbl is expressed at a high level in early embryos and throughout the imaginal discs in third instar larvae. This study forms the basis for future genetic analysis of DCbl, aimed at gaining insights into the role of Cbl proteins in signal transduction.

show abstract

Comparison of the consensus sequence flanking translational start sites inDrosophilaand vertebrates

Cited by 974 publications

References 38 publications

Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene

Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene

Cloning and characterization of the Drosophila homologue of the AP-2 transcription factor

D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites

Contact Info

Product

Resources

About