Recognition and long-range interactions of a minimal nanos RNA localization signal element

Development ◽  
2001 ◽  
Vol 128 (3) ◽  
pp. 427-435 ◽  
Author(s):  
S. Evans Bergsten ◽  
T. Huang ◽  
S. Chatterjee ◽  
E.R. Gavis
Keyword(s):  
Long Range ◽  
Germ Plasm ◽  
Rna Localization ◽  
Posterior Pole ◽  
Drosophila Embryo ◽  
Cis Acting ◽  
Signal Element ◽  
Long Range Interactions ◽  
Localization Signal ◽  
Localization Elements

Localization of nanos (nos) mRNA to the germ plasm at the posterior pole of the Drosophila embryo is essential to activate nos translation and thereby generate abdominal segments. nos RNA localization is mediated by a large cis-acting localization signal composed of multiple, partially redundant elements within the nos 3′ untranslated region. We identify a protein of approximately 75 kDa (p75) that interacts specifically with the nos +2′ localization signal element. We show that the function of this element can be delimited to a 41 nucleotide domain that is conserved between D. melanogaster and D. virilis, and confers near wild-type localization when present in three copies. Two small mutations within this domain eliminate both +2′ element localization function and p75 binding, consistent with a role for p75 in nos RNA localization. In the intact localization signal, the +2′ element collaborates with adjacent localization elements. We show that different +2′ element mutations not only abolish collaboration between the +2′ and adjacent +1 element but also produce long-range deleterious effects on localization signal function. Our results suggest that higher order structural interactions within the localization signal, which requires factors such as p75, are necessary for association of nos mRNA with the germ plasm.

Role for mRNA localization in translational activation but not spatial restriction of nanos RNA

Development ◽  
1999 ◽  
Vol 126 (4) ◽  
pp. 659-669 ◽  
Author(s):  
S.E. Bergsten ◽  
E.R. Gavis
Keyword(s):  
Translational Control ◽  
Rna Localization ◽  
Early Embryo ◽  
Posterior Pole ◽  
Translational Repression ◽  
Control Element ◽  
Regulatory Sequences ◽  
Cis Acting ◽  
Body Patterning ◽  
Localization Signal

Patterning of the anterior-posterior body axis during Drosophila development depends on the restriction of Nanos protein to the posterior of the early embryo. Synthesis of Nanos occurs only when maternally provided nanos RNA is localized to the posterior pole by a large, cis-acting signal in the nanos 3′ untranslated region (3′UTR); translation of unlocalized nanos RNA is repressed by a 90 nucleotide Translational Control Element (TCE), also in the 3′UTR. We now show quantitatively that the majority of nanos RNA in the embryo is not localized to the posterior pole but is distributed throughout the cytoplasm, indicating that translational repression is the primary mechanism for restricting production of Nanos protein to the posterior. Through an analysis of transgenes bearing multiple copies of nanos 3′UTR regulatory sequences, we provide evidence that localization of nanos RNA by components of the posteriorly localized germ plasm activates its translation by preventing interaction of nanos RNA with translational repressors. This mutually exclusive relationship between translational repression and RNA localization is mediated by a 180 nucleotide region of the nanos localization signal, containing the TCE. These studies suggest that the ability of RNA localization to direct wild-type body patterning also requires recognition of multiple, unique elements within the nanos localization signal by novel factors. Finally, we propose that differences in the efficiencies with which different RNAs are localized result from the use of temporally distinct localization pathways during oogenesis.

A conserved 90 nucleotide element mediates translational repression of nanos RNA

Development ◽  
1996 ◽  
Vol 122 (9) ◽  
pp. 2791-2800 ◽  
Author(s):  
E.R. Gavis ◽  
L. Lunsford ◽  
S.E. Bergsten ◽  
R. Lehmann
Keyword(s):  
Translational Control ◽  
Untranslated Region ◽  
Translational Regulation ◽  
Critical Role ◽  
Rna Localization ◽  
Translational Repression ◽  
Regulatory Function ◽  
Control Element ◽  
Cis Acting ◽  
Localization Signal

Correct formation of the Drosophila body plan requires restriction of nanos activity to the posterior of the embryo. Spatial regulation of nanos is achieved by a combination of RNA localization and localization-dependent translation such that only posteriorly localized nanos RNA is translated. Cis-acting sequences that mediate both RNA localization and translational regulation lie within the nanos 3′ untranslated region. We have identified a discrete translational control element within the nanos 3′ untranslated region that acts independently of the localization signal to mediate translational repression of unlocalized nanos RNA. Both the translational regulatory function of the nanos 3′UTR and the sequence of the translational control element are conserved between D. melanogaster and D. virilis. Furthermore, we show that the RNA helicase Vasa, which is required for nanos RNA localization, also plays a critical role in promoting nanos translation. Our results specifically exclude models for translational regulation of nanos that rely on changes in polyadenylation.

Distribution of tudor protein in the Drosophila embryo suggests separation of functions based on site of localization

Development ◽  
1993 ◽  
Vol 119 (1) ◽  
pp. 207-219 ◽  
Author(s):  
A. Bardsley ◽  
K. McDonald ◽  
R.E. Boswell
Keyword(s):  
Germ Cell ◽  
Germ Cells ◽  
Germ Plasm ◽  
Primordial Germ Cells ◽  
Posterior Pole ◽  
Drosophila Embryo ◽  
Normal Functioning ◽  
Polar Granules ◽  
Pole Cells

Mutations in the tudor locus of Drosophila affect two distinct determinative processes in embryogenesis; segmentation of the abdomen and determination of the primordial germ cells. The distribution of tudor protein during embryogenesis, and the effect of various mutations on its distribution, suggest that tudor protein may carry out these functions separately, based on its location in the embryo. The protein is concentrated in the posterior pole cytoplasm (germ plasm), where it is found in polar granules and mitochondria. Throughout the rest of the embryo, tudor protein is associated with the cleavage nuclei. Mutations in all maternal genes known to be required for the normal functioning of the germ plasm eliminate the posterior localization of tudor protein, whereas mutations in genes required for the functioning of the abdominal determinant disrupt the localization around nuclei. Analysis of embryos of different maternal genotypes indicates that the average number of pole cells formed is correlated with the amount of tudor protein that accumulates in the germ plasm. Our results suggest that tudor protein localized in the germ plasm is instrumental in germ cell determination, whereas nuclear-associated tudor protein is involved in determination of segmental pattern in the abdomen.

scholarly journals Community effects in regulation of translation

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Paul M Macdonald ◽  
Matt Kanke ◽  
Andrew Kenny
Keyword(s):  
Long Range ◽  
Translational Regulation ◽  
Regulatory Elements ◽  
Community Effects ◽  
Particle Assembly ◽  
Cis Acting ◽  
Long Range Interactions ◽  
In Trans ◽  
Single Transcript ◽  
In Cis

Certain forms of translational regulation, and translation itself, rely on long-range interactions between proteins bound to the different ends of mRNAs. A widespread assumption is that such interactions occur only in cis, between the two ends of a single transcript. However, certain translational regulatory defects of the Drosophila oskar (osk) mRNA can be rescued in trans. We proposed that inter-transcript interactions, promoted by assembly of the mRNAs in particles, allow regulatory elements to act in trans. Here we confirm predictions of that model and show that disruption of PTB-dependent particle assembly inhibits rescue in trans. Communication between transcripts is not limited to different osk mRNAs, as regulation imposed by cis-acting elements embedded in the osk mRNA spreads to gurken mRNA. We conclude that community effects exist in translational regulation.

Two copies of a subelement from the Vg1 RNA localization sequence are sufficient to direct vegetal localization in Xenopus oocytes

Development ◽  
1997 ◽  
Vol 124 (24) ◽  
pp. 5013-5020 ◽  
Author(s):  
D. Gautreau ◽  
C.A. Cote ◽  
K.L. Mowry
Keyword(s):  
Xenopus Oocytes ◽  
Rna Localization ◽  
Sequence Motifs ◽  
Sequence Element ◽  
Cis Acting ◽  
Vegetal Cortex ◽  
Sequence Elements ◽  
Localization Sequence ◽  
Localization Signal ◽  
Localization Element

Localization of mRNA has emerged as a fundamental mechanism for generating polarity during development. In vertebrates, one example of this phenomenon is Vg1 RNA, which is localized to the vegetal cortex of Xenopus oocytes. Vegetal localization of Vg1 RNA is directed by a 340-nt sequence element contained within its 3′ untranslated region. To investigate how such cis-acting elements function in the localization process, we have undertaken a detailed analysis of the precise sequence requirements for vegetal localization within the 340-nt localization element. We present evidence for considerable redundancy within the localization element and demonstrate that critical sequences lie at the ends of the element. Importantly, we show that a subelement from the 5′ end of the Vg1 localization element is, when duplicated, sufficient to direct vegetal localization. We suggest that the Vg1 localization element is composed of smaller, redundant sequence motifs and identify one such 6-nt motif as essential for localization. These results allow insight into what constitutes an RNA localization signal and how RNA sequence elements may act in the localization process.

scholarly journals Structural Changes in the Acceptor Site of Photosystem II upon Ca2+/Sr2+ Exchange in the Mn4CaO5 Cluster Site and the Possible Long-Range Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Long Range ◽  
Electron Acceptor ◽  
Structural Changes ◽  
Acceptor Site ◽  
Oxygen Evolving Complex ◽  
Long Range Interactions ◽  
Structural Perturbations ◽  
Oxygen Evolving

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.

scholarly journals Quantum Criticality of Two-Dimensional Quantum Magnets with Long-Range Interactions

2019 ◽  
Vol 122 (1) ◽  
Author(s):  
Sebastian Fey ◽  
Sebastian C. Kapfer ◽  
Kai Phillip Schmidt
Keyword(s):  
Long Range ◽  
Quantum Criticality ◽  
Two Dimensional ◽  
Quantum Magnets ◽  
Long Range Interactions
Sign in / Sign up

Export Citation Format

Share Document