Stronger induction of callose deposition in barley by Russian wheat aphid than bird cherry-oat aphid is not associated with differences in callose synthase or ≤-1,3-glucanase expression
- Authors: Saheed, Sefiu A , Cierlik, Izabela , Larsson, Kristina A E , Delp, Gabriele , Bradley, Graeme , Jonsson, Lisbeth M V , Botha, Christiaan E J
- Date: 2009
- Language: English
- Type: Article
- Identifier: vital:6542 , http://hdl.handle.net/10962/d1005984
- Description: The effects of infestation by the bird cherry-oat aphid (BCA), (Rhopalosiphum padi L) and the Russian wheat aphid (RWA) (Diuraphis noxia Mordvilko) on callose deposition and gene expression related to callose accumulation were investigated in barley (Hordeum vulgare L. cv. Clipper). The BCA, which gives no visible symptoms, induced very limited callose deposition, even after 14 days of infestation. In contrast, RWA, which causes chlorosis, white and yellow streaking and leaf rolling, induced callose accumulation already after 24h in longitudinal leaf veins. The deposition was pronounced after 72 h, progressing during 7 and 14 days of infestation. In RWA-infested source leaves, callose was also induced in longitudinal veins basipetal to the aphid-infested tissue, whereas in sink leaves, more callose deposition was found above the feeding sites. Nine putative callose synthase genes were identified in a data base search, of which eight were expressed in the leaves, but with similar level of expression in control and aphid-infested tissue. Four out of 12 examined β-1,3-glucanases were expressed in the leaves, and three of them were up-regulated in aphid-infested tissue. They were all more strongly induced by RWA than BCA. The results suggest that callose accumulation may be partly responsible for the symptoms resulting from RWA feeding and that a callose-inducing signal may be transported in the phloem. Furthermore it is concluded that the absence of callose deposition in BCA-infested leaves is not due to a stronger induction of callose-degrading β-1,3-glucanases in this tissue, as compared to RWA-infested leaves.
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- Date Issued: 2009
Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding
- Authors: Daniel, Sheril , Bradley, Graeme , Longshaw, Victoria M , Söti, Csaba , Csermely, Peter , Blatch, Gregory L
- Date: 2008
- Language: English
- Type: Article
- Identifier: vital:6472 , http://hdl.handle.net/10962/d1005951 , http://dx.doi.org/10.1016/j.bbamcr.2008.01.014
- Description: The Hsp70–Hsp90 complex is implicated in the folding and regulation of numerous signaling proteins, and Hop, the Hsp70–Hsp90 Organizing Protein, facilitates the association of this multichaperone machinery. Phosphatase treatment of mouse cell extracts reduced the number of Hop isoforms compared to untreated extracts, providing the first direct evidence that Hop was phosphorylated in vivo. Furthermore, surface plasmon resonance (SPR) spectroscopy showed that a cdc2 kinase phosphorylation mimic of Hop had reduced affinity for Hsp90 binding. Hop was predominantly cytoplasmic, but translocated to the nucleus in response to heat shock. A putative bipartite nuclear localization signal (NLS) has been identified within the Hsp90-binding domain of Hop. Although substitution of residues within the major arm of this proposed NLS abolished Hop–Hsp90 interaction as determined by SPR, this was not sufficient to prevent the nuclear accumulation of Hop under leptomycin-B treatment and heat shock conditions. These results showed for the first time that the subcellular localization of Hop was stress regulated and that the major arm of the putative NLS was not directly important for nuclear translocation but was critical for Hop–Hsp90 association in vitro. We propose a model in which the association of Hop with Hsp90 and the phosphorylated status of Hop both play a role in the mechanism of nucleo-cytoplasmic shuttling of Hop.
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- Date Issued: 2008
Molecular chaperones in biology, medicine and protein biotechnology
- Authors: Boshoff, Aileen , Nicoll, William S , Hennessy, Fritha , Ludewig, M H , Daniel, Sheril , Modisakeng, Keoagile W , Shonhai, Addmore , McNamara, Caryn , Bradley, Graeme , Blatch, Gregory L
- Date: 2004
- Language: English
- Type: Article
- Identifier: vital:6457 , http://hdl.handle.net/10962/d1004479
- Description: Molecular chaperones consist of several highly conserved families of proteins, many of which consist of heat shock proteins. The primary function of molecular chaperones is to facilitate the folding or refolding of proteins, and therefore they play an important role in diverse cellular processes including protein synthesis, protein translocation, and the refolding or degradation of proteins after cell stress. Cells are often exposed to different stressors, resulting in protein misfolding and aggregation. It is now well established that the levels of certain molecular chaperones are elevated during stress to provide protection to the cell. The focus of this review is on the impact of molecular chaperones in biology, medicine and protein biotechnology, and thus covers both fundamental and applied aspects of chaperone biology. Attention is paid to the functions and applications of molecular chaperones from bacterial and eukaryotic cells, focusing on the heat shock proteins 90 (Hsp90), 70 (Hsp70) and 40 (Hsp40) classes of chaperones, respectively. The role of these classes of chaperones in human diseases is discussed, as well as the parts played by chaperones produced by the causative agents of malaria and trypanosomiasis. Recent advances have seen the application of chaperones in improving the yields of a particular target protein in recombinant protein production. The prospects for the targeted use of molecular chaperones for the over-production of recombinant proteins is critically reviewed, and current research on these chaperones at Rhodes University is also discussed.
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- Date Issued: 2004