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Magaji G. Usman, Mohd Y. Rafii, Mohd Razi Ismail, Mohammad Abdul Malek, and Mohammad Abdul Latif

area of research. Heat shock proteins (HSPs), or stress proteins, are highly conserved and present in all plants and animals. Previous results revealed that most HSPs serve as molecular chaperones ( Bukau et al., 2006 ; Pratt et al., 2001 ). These

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Mark A. Ritenour, Sunita Kochhar, Larry E. Schrader, Tsui-Ping Hsu, and Maurice S.B. Ku

Washington State Tree Fruit Research Commission. We also thank Elizabeth Vierling at the University of Arizona for generous donations of anti-HSP18.1 antibodies from pea and antiwheat HSP70 antibodies. The cost of publishing this paper was defrayed in part by

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Emily B. Merewitz, Thomas Gianfagna, and Bingru Huang

transformed a widely used cool-season turfgrass species, creeping bentgrass, using the ipt gene ligated to a senescence-associated promoter, SAG12 ( Gan and Amasino, 1995 ) and a heat shock promoter, HSP18.2 ( Takahashi and Komeda, 1989 ). The senescence

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Janet Slovin

Our lab has initiated a project to determine if specific proteins expressed by strawberry function as part of the thermotolerance system. We have developed tools for investigating the role of heat shock proteins (HSPs) and other gene products in strawberry thermotolerance. These tools include an inbred diploid testing system, EST sequence data, and molecular markers for heat tolerance. We developed an inbred line, 5AF7, of the diploid strawberry Fragariavesca for testing gene function because the diploid genome is small (164Mbp), the life cycle of the plant is short (about 4 months), the plant size is small (a plant will produce fruit in a 4-inch pot), some genetic work is already done, F. vesca is transformable with Agrobacteriumtumefaciens, and results should be transferable to the commercial octoploid varieties. A cDNA library was constructed in the pCMVsport 6.1 vector using combined RNA from batches of aseptically grown F. vesca seedlings treated to various elevated temperature regimes. Over 1500 EST sequences from the library have been deposited in GenBank and are available annotated at the ESTAP Fragaria database (http://staff.vbi.vt.edu/estap/index.shtml). HSP101 affects thermotolerance in Arabidopsis(Queitsch et al., 2000, Plant Cell 12:479). A PCR fragment for HSP101 was generated from F. vesca with degenerate primers, and used to obtain a full-length cDNA clone from the library. Primers spanning an intron were designed for RTPCR from the sequence of the cDNA. Semi-quantitative RTPCR indicates that HSP101 is expressed constitutively in young leaves at 25 °C and is not induced at moderately higher temperatures (32 °C) even after 5 hours. Induction occurs within 1 hour at 37 °C.

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Konstantinos E. Vlachonasios, Dina K. Kadyrzhanova, and David R. Dilley

Heat-treatment of mature-green tomato fruit (Lycopersicon esculentum) for 48 h at 42°C has been shown to prevent chilling injury from developing after 2 or 3 weeks at 2°C. Using mRNA differential display, we recently cloned and characterized a cDNA that encodes a cytosolic class II small heat-shock protein (Le HSP17.6). The mRNA of Le HSP17.6 is up-regulated during heat shock and the level of transcription remains high during subsequent storage at chilling temperatures. We used mRNA differential display with gene-specific primers from the other small HSPs families and find that the transcription of the other small heat-shock proteins is up-regulated during heat shock and persists at elevated levels at 2°C for at least 2 weeks. When the fruits are returned to a permissive ripening temperature after the chilling period, the mRNA of the small HSPs declines slowly for 3 days. These results suggest that the persistence of the small heat-shock proteins at low temperatures may provide protection against chilling injury.

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Hyesoon Kim and Yeh-Jin Ahn

stress. All living organisms, including plants, respond to heat stress (10 to 15 °C above their optimal growth temperatures) by producing a set of proteins called heat shock proteins (HSPs; Wahid et al., 2007 ). In eukaryotic organisms, HSPs are

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Paul H. Jennings and Ann Fitzpatrick

Heat shock induction of chilling tolerance in cucumber seedlings is not blocked by inhibitors of protein synthesis. Treatment of germinating seeds with cycloheximide and actinomycin-D, prior to heat shock and chilling, does not block the heat shock induction of chilling tolerance, while the inhibitors alone promote chilling tolerance of seedling roots. To test whether the heat shock effect might be acting on proteases, two protease inhibitors (bestatin and PMSF) were tested for their ability to induce chilling tolerance. Although PMSF slowed germination, it still provided protection against chilling, but bestatin was much more effective.

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Hanseul Park and Yeh-Jin Ahn

growth. In the present study, we aimed to recombine a small heat shock protein gene, Hsp17.7 , from carrot ( D. carota ‘Mussangochon’) into the E. coli chromosome to increase the tolerance to adverse cultural conditions. Small heat shock proteins

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Allan B. Woolf, Christopher B. Watkins, Judith H. Bowen, Michael Lay-Yee, John H. Maindonald, and Ian B. Ferguson

. Spooner and thank L. Nover (Halle, Germany) for the gifts of the hsp cDNA clones. Special thanks to A. Gunson and S. Bamett for assistance with statistical analyses and graphs. The cost of publishing this paper was defrayed in part by the payment of page

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Allan B. Woolf and Michael Lay-Yee

We wish to thank D. Mandino and L. Batt for supply of fruit and L. Nover (Halle, Germany) for the gifts of the hsp cDNA clones. We also thank J. Bowen and K. Spooner for excellent technical assistance and J. Maindonald, A. Gunson, and S. Barnett