Upstream Sequences Other than AAUAAA Are Required for Efficient Messenger RNA 3'-End Formation in Plants

Mogen, Bradley D.; MacDonald, Margaret H.; Graybosch, Robert A.; Hunt, Arthur G.

doi:10.2307/3869344

Cited by 37 publications

(89 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Differences in the lengths of the 3'-UTR have also been reported in serine proteinases from other fungi (Kingsnorth et al 2001). Determination of the polyadenylation signal sequence at the 3'-UTR was rather difficult because it did not follow the general consensus sequence AAUAAA (Mogen et al 1990). Plant genes have also been reported to have no sharply defined consensus sequence for polyadenylation signal (Li and Hunt, 1995).…”

Section: Discussionmentioning

confidence: 94%

Molecular cloning, expression and characterization of a serine proteinase from Japanese edible mushroom, Grifola frondosa: solving the structure - function anomaly of a reported aminopeptidase

Islam¹

2008

Electron. J. Biotechnol.

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 94%

Molecular cloning, expression and characterization of a serine proteinase from Japanese edible mushroom, Grifola frondosa: solving the structure - function anomaly of a reported aminopeptidase

Islam¹

2008

Electron. J. Biotechnol.

View full text Add to dashboard Cite

“…D, Some single-nucleotide mutations resulted in little structural changes, as well as signal efficiencies. *, The mutations and signal usage efficiencies were measured from the data presented by Rothnie et al (1994) for A, B, and D and Mogen et al (1990) for A and C, respectively. Free energy is 2187 for all structures.…”

Section: Discussionmentioning

confidence: 99%

“…6B). Moreover, when 3 of the 6 nt were changed (from AAUAAA to UAGAAU), the efficiency of the signal was reduced to 51% calculated from the band intensity of the S1 nuclease protection assay (figure 3 in Mogen et al, 1990), and the structural change is visible (Fig. 6C).…”

Section: Mutagenesis Data Support the Existence Of The Predicted Secomentioning

confidence: 99%

Compilation of mRNA Polyadenylation Signals in Arabidopsis Revealed a New Signal Element and Potential Secondary Structures

et al. 2005

View full text Add to dashboard Cite

Using a novel program, SignalSleuth, and a database containing authenticated polyadenylation [poly(A)] sites, we analyzed the composition of mRNA poly(A) signals in Arabidopsis (Arabidopsis thaliana), and reevaluated previously described cis-elements within the 3#-untranslated (UTR) regions, including near upstream elements and far upstream elements. As predicted, there are absences of high-consensus signal patterns. The AAUAAA signal topped the near upstream elements patterns and was found within the predicted location to only approximately 10% of 3#-UTRs. More importantly, we identified a new set, named cleavage elements, of poly(A) signals flanking both sides of the cleavage site. These cis-elements were not previously revealed by conventional mutagenesis and are contemplated as a cluster of signals for cleavage site recognition. Moreover, a singlenucleotide profile scan on the 3#-UTR regions unveiled a distinct arrangement of alternate stretches of U and A nucleotides, which led to a prediction of the formation of secondary structures. Using an RNA secondary structure prediction program, mFold, we identified three main types of secondary structures on the sequences analyzed. Surprisingly, these observed secondary structures were all interrupted in previously constructed mutations in these regions. These results will enable us to revise the current model of plant poly(A) signals and to develop tools to predict 3#-ends for gene annotation.Messenger RNA polyadenylation is a crucial step during the maturation of most eukaryotic mRNA, in which a polyadenine [poly(A)] tract is added to the cleaved 3#-end of a precursor mRNA (pre-mRNA) posttranscriptionally. Such a modification of mRNA has been shown to affect its stability, translatability, and nuclear-to-cytoplasmic export (Zhao et al., 1999). The posttranscriptional processing of mRNA is an event that has also been found tightly coupled with splicing and transcription termination (Proudfoot et al., 2002;Proudfoot, 2004). Thus, it is an essential processing event and the integral part of gene expression.The polyadenylation process requires two major components: the cis-elements or poly(A) signals of the pre-mRNA, and the trans-acting factors that carry out the cleavage and addition of the poly(A) tail at the 3#-end. These trans-acting factors are a complex of about 25 to 30 proteins involved in signal recognition, cleavage, and polyadenylation (Proudfoot, 2004). These proteins seem to be conserved among eukaryotic organisms. However, the poly(A) signals have been found to differ widely among yeast (Saccharomyces cerevisiae), animals, and plants in terms of signal locations and sequence content. The highly conserved AAUAAA element in mammals becomes a minor signal in plant and yeast genes, and the ubiquitous downstream elements of mammalian pre-mRNAs are nowhere to be found in yeast and plants. The latter two possess an enhancing element located far upstream of the cleavage site (Zhao et al., 1999).Previous understanding of these signal elements was derived mostly...

show abstract

“…The 190-bp 3' untranslated sequence contained two poly(A) addition signals (AATAA) at positions -140 and -90 relative to the poly(A) tail. This is relatively distant for the position of the classical poly(A) addition signal from the actual poly(A) tail in higher eukaryotes, so potentially nonconsensus poly(A) sites are used (Mogen et al, 1990). The SPS cDNA was used as a probe to detect SPS transcripts.…”

Section: Maize Sps 1s Encoded By a 3500-bp Mrnamentioning

confidence: 99%

Expression of a Maize Sucrose Phosphate Synthase in Tomato Alters Leaf Carbohydrate Partitioning

Worrell¹,

Bruneau²,

Summerfelt³

et al. 1991

The Plant Cell

View full text Add to dashboard Cite

We isolated a complementary DNA sequence for the enzyme sucrose phosphate synthase (SPS) from maize utilizing a limited amino acid sequence. The 3509-bp cDNA encodes a 1068-amino acid polypeptide. The identity of the cDNA was confirmed by the ability of the cloned sequence to direct sucrose phosphate synthesis in Escherichia coli. Because no plant-specific factors were necessary for enrymatic activity, we can conclude that SPS enzyme activity is conferred by a single gene product. Sequence comparisons showed that SPS is distantly related to the enzyme sucrose synthase. When expressed from a ribulose bisphosphate carboxylase small subunit promoter in transgenic tomatoes, total SPS activity was boosted up to sixfold in leaves and appeared to be physiologically uncoupled from the tomato regulation mechanism. The elevated SPS activity caused a reduction of starch and increase of sucrose in the tomato leaves. This result clearly demonstrates that SPS is involved in the regulation of carbon partitioning in the leaves.

show abstract

Upstream Sequences Other than AAUAAA Are Required for Efficient Messenger RNA 3'-End Formation in Plants

Cited by 37 publications

References 11 publications

Molecular cloning, expression and characterization of a serine proteinase from Japanese edible mushroom, Grifola frondosa: solving the structure - function anomaly of a reported aminopeptidase

Molecular cloning, expression and characterization of a serine proteinase from Japanese edible mushroom, Grifola frondosa: solving the structure - function anomaly of a reported aminopeptidase

Compilation of mRNA Polyadenylation Signals in Arabidopsis Revealed a New Signal Element and Potential Secondary Structures

Expression of a Maize Sucrose Phosphate Synthase in Tomato Alters Leaf Carbohydrate Partitioning

Contact Info

Product

Resources

About