Eukaryotic start and stop translation sites

Cavener, Douglas R.; Ray, Stuart C.

doi:10.1093/nar/19.12.3185

Cited by 582 publications

(395 citation statements)

References 33 publications

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“…The longest ORF of the 5.0-kb RNA begins at a methionine codon at genomic nucleotide +2163 and continues for 1,028 codons. This AUG codon is not, however, in a good translation initiation context (7). The putative 5' untranslated region of 1,169 to 1,193 nucleotides, depending on whether exon la or exon lb has been joined to exon 2, contains four short ORFs that have AUG start codons and in-frame termination codons three to nine triplets downstream; none of these termination codons are in the same reading frame as the longest ORF.…”

Section: Resultsmentioning

confidence: 98%

Multiple products from the shavenbaby-ovo gene region of Drosophila melanogaster: relationship to genetic complexity.

Garfinkel¹,

Wang²,

Liang³

et al. 1994

Mol. Cell. Biol.

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The Drosophila melanogaster shavenbaby (svb)-ovo gene region is a complex locus, containing two distinct but comutable genetic functions. ovo is required for survival and differentiation of female germ line cells and plays a role in germ line sex determination. In contrast, svb is required in both male and female embryos for the production of epidermal locomotor and sensory structures. Sequences required for the two genetic functions are partially overlapping. ovo corresponds to a previously described germ line-dependent 5.0-kb poly(A)+ mRNA that first appears in the germarium and accumulates in nurse cells during oogenesis. The 5.0-kb mRNA is stored in the egg, but it is rapidly lost in the embryos except for its continued presence in the germ line precursor pole cells. The ovo mRNA predicts a 1,028-amino-acid 110.6-kDa protein homologous with transcription factors. We have identified an embryonic mRNA, 7.1 kb in length, that contains exons partially overlapping those of the 5.0-kb poly(A)+ mRNA. The spatial distribution of this newly discovered transcript during midembryogenesis suggests that it corresponds to the svb function. The arrangement of exons common to the 5.0-and 7.1-kb mRNAs suggests that the Ovo and Svb proteins share DNA-binding specificity conferred by four Cys2-His2 zinc finger motifs but differ functionally in their capacity to interact with other components of the transcription machinery.The central role of Sex-lethal (Sxl) for sex determination in the somatic tissues of Drosophila melanogaster has been elegantly worked out (reviewed in reference 9). However, the mechanisms active in the germ line differ in three major ways from those operating in somatic sex determination. First, although Sxl is required in the germ line, it is not active in the germ line precursor cells of early embryos (4) when sex-specific germ line functions first appear. Second, the activation of Sxl in the germ line does not require the same X-linked genes as required for its activation in embryonic somatic cells (14, 37), nor are the downstream genes required in the germ line (reviewed in references 28 and 36). Third, germ line sex determination is not autonomous but depends upon proper somatic cell-germ line interactions (38). Thus, it is necessary to identify the genes required by germ line cells for the assessment of sex identity and to determine the biochemical pathways by which they operate.A key gene for sex-dimorphic germ line functions is ovo. Recessive, apparently null, alleles cause female-specific sterility due to the loss of germ cells in the embryo (27 ovo alleles to suppress partially P-M hybrid dysgenesisinduced female germ line cell death (39). Thus, ovo appears to play a prominent role in the early female-specific establishment of the germ line as well as in subsequent oocyte development and differentiation.Genomic DNA sequences required for ovo function are genetically overlapping and interdigitated with the genomic DNA sequences required for the shavenbaby (svb) function (13,22). svb is known to aff...

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Section: Resultsmentioning

confidence: 98%

Multiple products from the shavenbaby-ovo gene region of Drosophila melanogaster: relationship to genetic complexity.

Garfinkel¹,

Wang²,

Liang³

et al. 1994

Mol. Cell. Biol.

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“…(1) TIS organization in mRNAs of monocot plants resembles that of mammals (consensus: GCRGCARCCAUGGC), whereas mRNAs of dicot plants differ considerably (consensus: AAAAAAAAMAUGGC). (5) It was demonstrated that the most-important positions in plant mRNAs are also À3 and þ4; the other important positions are À2, À1, þ5. GCCAUGGC and RAAAUGGC were shown to be the most-efficient TISs in maize and tobacco cells, respectively.…”

Section: Eukaryotic Mrnas and Translation Initiation Mechanismsmentioning

confidence: 99%

Alternative translation start sites and hidden coding potential of eukaryotic mRNAs

2008

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SummaryIt is widely suggested that a eukaryotic mRNA typically contains one translation start site and encodes a single functional protein product. However, according to current points of view on translation initiation mechanisms, eukaryotic ribosomes can recognize several alternative translation start sites and the number of experimentally verified examples of alternative translation is growing rapidly. Also, the frequent occurrence of alternative translation events and their functional significance are supported by the results of computational evaluations. The functional role of alternative translation and its contribution to eukaryotic proteome complexity are discussed.

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“…First, an oligonucleotide containing the ribosome binding site (Kozac) consensus sequence for Drosophila (Cavener and Ray, 1991) and an N-terminal sequence encoding MARGS(his)6 was introduced into the unique EcoRI site of pCaSpeR-hs. This fragment was generated by annealing and extending the following primers: 5′ CCG CGG AAT TCA CAA CCA AAA TGG CGA GAG GAT CGC ATC 3′ and 5′ GGC CGA ATT CGG TAC CGT GAT GGT GAT GGT GAT GCG ATC C 3′, to generate an EcoRI-Kozac-MARGS(his)6-KpnI-EcoRI-containing oligonucleotide, which was restricted with EcoRI, PAGE-purified and cloned into pCaSpeR-hs.…”

Section: Plasmid Constructionmentioning

confidence: 99%

Quantitative contributions of CtBP-dependent and -independent repression activities of Knirps

et al. 2004

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The Drosophila Knirps protein is a short-range transcriptional repressor that locally inhibits activators by recruiting the CtBP co-repressor. Knirps also possesses CtBP-independent repression activity. The functional importance of multiple repression activities is not well understood, but the finding that Knirps does not repress some cis-regulatory elements in the absence of CtBP suggested that the co-factor may supply a unique function essential to repress certain types of activators. We assayed CtBP-dependent and -independent repression domains of Knirps in Drosophila embryos, and found that the CtBPindependent activity, when provided at higher than normal levels, can repress an eve regulatory element that normally requires CtBP. Dose response analysis revealed that the activity of Knirps containing both CtBP-dependent and -independent repression activities is higher than that of the CtBP-independent domain alone. The requirement for CtBP at certain enhancers appears to reflect the need for overall higher levels of repression, rather than a requirement for an activity unique to CtBP. Thus, CtBP contributes quantitatively, rather than qualitatively, to overall repression function. The finding that both repression activities are simultaneously deployed suggests that the multiple repression activities do not function as cryptic 'backup' systems, but that each contributes quantitatively to total repressor output.

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Eukaryotic start and stop translation sites

Cited by 582 publications

References 33 publications

Multiple products from the shavenbaby-ovo gene region of Drosophila melanogaster: relationship to genetic complexity.

Multiple products from the shavenbaby-ovo gene region of Drosophila melanogaster: relationship to genetic complexity.

Alternative translation start sites and hidden coding potential of eukaryotic mRNAs

Quantitative contributions of CtBP-dependent and -independent repression activities of Knirps

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