The Molecular Chaperone Hsp90 Is Required for mRNA Localization in <i>Drosophila melanogaster</i> Embryos

Song, Yan; Fee, Lanette; Lee, Tammy H.; Wharton, Robin P.

doi:10.1534/genetics.107.071472

Cited by 30 publications

(25 citation statements)

References 69 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although this graph was corrected for non-linearity of the staining method, it is not consistent with our analysis using modern experimental and analytical tools (see below). In addition, in some cases a bcd mRNA gradient can indeed be observed but was missed or ignored (T. Berleth, PhD thesis, University of Tübingen, 1988) (Berleth et al, 1988;St Johnston et al, 1989;Schnorrer et al, 2002;Song et al, 2007).…”

Section: Revisiting the Bcd Mrna Gradientmentioning

confidence: 99%

Formation of thebicoidmorphogen gradient: an mRNA gradient dictates the protein gradient

et al. 2009

View full text Add to dashboard Cite

The Bicoid (Bcd) protein gradient is generally believed to be established in pre-blastoderm Drosophila embryos by the diffusion of Bcd protein after translation of maternal mRNA, which serves as a strictly localized source of Bcd at the anterior pole. However, we previously published evidence that the Bcd gradient is preceded by a bcd mRNA gradient. Here, we have revisited and extended this observation by showing that the bcd mRNA and Bcd protein gradient profiles are virtually identical at all times. This confirms our previous conclusion that the Bcd gradient is produced by a bcd mRNA gradient rather than by diffusion. Based on our observation that bcd mRNA colocalizes with Staufen (Stau), we propose that the bcd mRNA gradient forms by a novel mechanism involving quasi-random active transport of a Stau-bcd mRNA complex through a nonpolar microtubular network, which confines the bcd mRNA to the cortex of the embryo.

show abstract

Section: Revisiting the Bcd Mrna Gradientmentioning

confidence: 99%

Formation of thebicoidmorphogen gradient: an mRNA gradient dictates the protein gradient

et al. 2009

View full text Add to dashboard Cite

show abstract

“…HSP90 is also required for normal spermatogenesis, oogenesis, and embryogenesis in Drosophila spp. (Yue et al 1999;Song et al 2007;Pisa et al 2009). Recent studies have confirmed that HSP90 has been thought to have evolutionarily conserved functions that contribute to oogenesis and compound eye development in the red flour beetle Tribolium castaneum (Xu et al 2010;Knorr and Vilcinskas 2011).…”

Section: Introductionmentioning

confidence: 99%

Characterizing heat shock protein 90 gene of Apolygus lucorum (Meyer-Dür) and its expression in response to different temperature and pesticide stresses

Sun

Sheng

Bai

et al. 2014

Cell Stress and Chaperones

View full text Add to dashboard Cite

In this study, we cloned a full-length cDNA of heat shock protein (HSP) gene of Apolygus lucorum (Meyer-Dür) [AlHSP90, KC109781] and investigated its expression in response to temperature and pesticide stresses. The open reading frame (ORF) of AlHSP90 is 2,169 bp in length, encoding a 722 amino acid polypeptide with a predicted molecular weight of 82.99 kDa. Transcriptional and translational expression profiles of AlHSP90 under extreme temperature or pesticide stresses were examined by fluorescent realtime quantitative PCR and Western blot. Results showed that the expression profiles of AlHSP90 protein were in high agreement with those of AlHSP90 RNA and indicated that AlHSP90 was not only an important gene for A. lucorum adults in response to extremely high temperature, but also involved in the resistance or tolerance to cyhalothrin, imidacloprid, chlorpyrifos, and emamectin benzoate, especially for female adults to emamectin benzoate and for male adults to cyhalothrin. Transcriptional results of AlHSP90 also confirmed that AlHSP90 was an important gene involved in the resistance or tolerance to both temperature and pesticide stresses. In addition, our study also revealed that ∼24°C may be the suitable temperature range for A. lucorum survival, which is also confirmed by the results of the expression of AlHSP90, the nymph mortality, and the intrinsic rate of increase (r m ) when A. lucorum is reared at six different temperatures. Therefore, these studies are significant in elucidating the AlHSP90 in response to temperature and pesticide stresses and would provide guidance for A. lucorum management with different pesticides or temperatures in fields.

show abstract

“…Although mutations that cause defects in nos localization have been identified in numerous genetic screens, the effects of these mutations on nos are most likely to be indirect, as they disrupt localization or assembly of germ plasm. A recent genetic screen for nos localization factors identified the chaperone Hsp90 (also known as Hsp83 -FlyBase) as being important for nos localization, though its role also appears to be indirect (Song et al, 2007). Given the redundancy within the nos localization signal and, consequently, the potential for functional redundancy among proteins that interact with different nos localization elements, genetic approaches may fail to identify direct-acting localization factors.…”

Section: Introductionmentioning

confidence: 99%

TheDrosophilahnRNP M homolog Rumpelstiltskin regulatesnanosmRNA localization

Jain

Gavis

2008

Development

View full text Add to dashboard Cite

Anterior-posterior axis patterning of the Drosophila embryo requires Nanos activity selectively in the posterior. This spatial asymmetry of Nanos is generated by the localization of nanos mRNA to the posterior pole of the embryo, where it is subsequently translated. Posterior localization of nanos is mediated by a complex cis-acting localization signal in its 3Ј untranslated region comprising several partially redundant localization elements. This localization signal redundancy has hampered the identification of trans-acting factors that act specifically to effect posterior localization of nanos. Here, we have used a biochemical approach to identify Rumpelstiltskin, a Drosophila heterogeneous nuclear ribonucleoprotein (hnRNP) M homolog, which binds directly to an individual nanos localization element. Rumpelstiltskin associates with nanos mRNA in vitro and in vivo, and binding by Rumpelstiltskin correlates with localization element function in vivo. Through analysis of a rumpelstiltskin null mutation by genetic strategies that circumvent redundancy, we demonstrate that Rumpelstiltskin regulates anterior-posterior axis patterning by functioning as a direct-acting nanos mRNA localization factor.

show abstract

The Molecular Chaperone Hsp90 Is Required for mRNA Localization in Drosophila melanogaster Embryos

Cited by 30 publications

References 69 publications

Formation of thebicoidmorphogen gradient: an mRNA gradient dictates the protein gradient

Formation of thebicoidmorphogen gradient: an mRNA gradient dictates the protein gradient

Characterizing heat shock protein 90 gene of Apolygus lucorum (Meyer-Dür) and its expression in response to different temperature and pesticide stresses

TheDrosophilahnRNP M homolog Rumpelstiltskin regulatesnanosmRNA localization

Contact Info

Product

Resources

About