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Conserved sequence elements in the 5′ region of the Ultrabithorax transcription unit
Author(s) -
Wilde C. Deborah,
Akam Michael
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02380.x
Subject(s) - ultrabithorax , drosophila pseudoobscura , biology , genetics , drosophila melanogaster , melanogaster , orfs , gene , hox gene , transcription factor , open reading frame , peptide sequence
Clones homologous to the 5′ region of the Ultrabithorax gene of Drosophila melanogaster have been isolated from D. pseudoobscura, D. funebris and Musca domestica . Regions that encode most of the Ubx protein have been sequenced in all three of these species, and the 5′ upstream region has been sequenced in D. funebris to a point ˜1000 bases upstream of the probable mRNA start site. Here we compare these sequences with those described elsewhere for D. melanogaster . Deduced amino acid sequences of the Ubx protein show 8% ( D. pseudoobscura ), 15% ( D. funebris ) and 22% ( M. domestica ) divergence from D. melanogaster . However, these figures mask very different rates of evolution in different regions of the protein. A glycine‐rich (‘hinge’) region is conserved in each of these species, although its length is variable. Comparison of D. funebris and D. melanogaster sequences in the long 5′ untranslated leader region of the mRNA, and in the region immediately upstream of the start point of transcription, reveals tightly conserved elements embedded in an otherwise non‐homologous sequence. These conserved elements include a 118‐bp region that spans the mRNA start site, an internally repetitive (TAA) n region in the untranslated leader and a short repeated motif immediately upstream of the ATG codon that initiates the major open reading frame of the Ubx protein. Two other conserved elements were identified upstream of the transcription start site; both elements have structural features consistent with a role as recognition sites for regulatory proteins.