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1

Electronic Resource

Heat shock proteins and effects of heat shock in plants (1982)

Altschuler, Mitchell ; Mascarenhas, Joseph P.

Springer

Plant molecular biology 1 (1982), S. 103-115

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ISSN: 1573-5028

Keywords: heat shock proteins ; soybean ; corn ; seed storage proteins ; functions

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Soybean seedlings when exposed to a heat shock respond in a manner very similar to that exhibited by cultured cells, and reported earlier [2]. Maximum synthesis of heat shock proteins (HSPs) occurs at 40C. The heat shock response is maintained for a relatively short time under continuous high temperature. After 2.5 hr at 40 C the synthesis of HSPs decreases reaching a very low level by 6 hr. The HSPs synthesized by cultured cells and seedlings are identical and there is a large degree of similarity in HSPs synthesized between the taxonomically widely separated species, soybean and corn. Storage protein synthesis in the developing soybean embryo is not inhibited but is actually stimulated during a heat shock, unlike most other non-HSPs, whose synthesis is greatly reduced. Seedlings respond differently to a gradual increase in temperature than they do a sudden heat shock. There is an upward shift of several degrees in the temperature at which maximum protein synthesis occurs and before it begins to be inhibited. In addition, there appears to be a protection of normal protein synthesis from heat shock inhibition when the temperature increase is gradual. An additional function of the heat shock phenomenon might be the protection of seedlings from death caused by extreme heat stress. The heat shock response appears to have relevance to plants in the field.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00024974

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2

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Transcription and translation of heat shock and normal proteins in seedlings and developing seeds of soybean exposed to a gradual temperature increase (1985)

Altschuler, Mitchell ; Mascarenhas, Joseph P.

Springer

Plant molecular biology 5 (1985), S. 291-297

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ISSN: 1573-5028

Keywords: actin ; heat shock proteins ; mRNAs ; storage proteins

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Heat shock proteins (hsps) are synthesized at higher temperatures in soybean seedlings exposed to a gradual temperature increase as compared to a rapid heat shock (hs). There are differences in the pattern of synthesis of different hsps depending on whether the temperature exposure is rapid or gradual. The synthesis of normal temperature proteins also occurs at higher temperatures after a gradual increase in temperature than after a rapid hs. The increased protein synthesis seen with a gradual temperature increase is because of increased mRNA levels. In general the mRNAs for actin and the hsps are found at temperatures 6 to 9°C higher after a gradual temperature increase than after a rapid hs. While hsps are detected in developing seeds after either type of heat treatment an increase in the synthesis of hsps is observed at the higher temperatures after a gradual temperature increase compared to a rapid hs to the same temperatures. The only proteins synthesized at the highest temperatures (49°C) after a gradual temperature increase are the precursors of the storage proteins and the hsps. After a gradual increase in temperature the mRNAs for the 11S storage proteins are present in relatively large amounts up to 43°C decreasing thereafter but were detectable at 52°C; whereas, the hsp mRNA levels were relatively constant from 40 to 52°C.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00020626

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3

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Two soybean seed lipoxygenase nulls accumulate reduced levels of lipoxygenase transcripts (1986)

Start, William G. ; Ma, Yu ; Polacco, Joseph C. ; [et al.]

Springer

Plant molecular biology 7 (1986), S. 11-23

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ISSN: 1573-5028

Keywords: cDNA ; Glycine max ; lipoxygenase ; lipoxygenase-null ; pUC8 expression vector ; seed protein

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Soybean (Glycine max L. [Merrill]) seed lipoxygenase cDNA clones were recovered from two cDNA libraries: a size-selected library in pBR322 and an expression library in pUC8. The pUC8 library was made with total poly(A)+ embryo RNA and was screened with antiserum to lipoxygenase-1, one of 3 seed lipoxygenase isozymes. Three lipoxygenase antigen-producing clones were identified: two with identical cDNA inserts of 977 nucleotides representing an open-reading frame and a third truncated clone bearing a 3′ end common to the longer clones. A long clone, pAL-134, was chosen for further study and was used to screen the size-selected cDNA library from which sixteen clones were identified. They fall into two homology classes represented by pLX-10 (ca. 1360 bp) and pLX-65 (2047 bp). The lipoxygenase expression clone pAL-134 hybridized much more strongly to pLX-65 than to pLX-10. pAL-134 and pLX-65 share 89% nucleotide homology and 75% deduced amino acid homology along their common sequence. Their deduced amino acid sequences each show 80% homology to sequences determined for isolated peptides of the lipoxygenase-1 isozyme. pAL-134 hybridizes poorly with a 3.8 kb RNA from LOX-1 null (lx1) embryos while pLX-65 hybridizes more strongly, but still to a lesser extent than its hybridization to standard embryo RNA or to RNA from embryos lacking lipoxygenase-2 (lx2) or lipoxygenase-3 (lx3) protein. The lx3 null lacks almost all embryo 3.8 kb RNA homologous to pLX-10. This hybridization pattern suggests that pLX-10 encodes LOX-3. Thus, the lx1 and lx3 genotypes accumulate little, if any, mRNA for the lipoxygenase-1 and lipoxygenase-3 isozymes, respectively.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00020127

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4

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Molecular cloning and expression of a MAP kinase homologue from pea (1993)

Stafstrom, Joel P. ; Altschuler, Mitchell ; Anderson, David H.

Springer

Plant molecular biology 22 (1993), S. 83-90

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ISSN: 1573-5028

Keywords: axillary bud development ; cell cycle regulation ; MAP kinase ; Pisum sativum ; protein kinase

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The cdc2 kinases are important cell cycle regulators in all eukaryotes. MAP kinases, a closely related family of protein kinases, are involved in cell cycle regulation in yeasts and vertebrates, but previously have not been documented in plants. We used PCR to amplify Brassica napus DNA sequences using primers corresponding to amino sequences that are common to all known protein kinases. One sequence was highly similar to KSS1, a MAP kinase from Saccharomyces cerevisiae. This sequence was used to isolate a full-length MAP kinase-like clone from a pea cDNA library. The pea clone, called D5, shared approximately 50% amino acid identity with MAP kinases from yeasts and vertebrates and about 41% identity with plant cdc2 kinases. An expression protein encoded by D5 was recognized by an antiserum specific to human MAP kinases (ERKs). Messenger RNA corresponding to D5 was present at similar levels in all tissues examined, without regard to whether cell division or elongation were occurring in those tissues.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00038997

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5

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Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific (1993)

Kenward, Kimberly D. ; Altschuler, Mitchell ; Hildebrand, David ; [et al.]

Springer

Plant molecular biology 23 (1993), S. 377-385

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ISSN: 1573-5028

Keywords: antifreeze proteins ; gene transfer ; preproprotein processing ; α-helix stability

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Expression of fish antifreeze protein (AFP) genes in plants is a possible means of increasing their frost resistance and freeze tolerance. Initial work involved transfer into tobacco of an AFP gene from winter flounder which codes for the alanine-rich, α-helical Type I AFP. Plants were transformed with a gene construct in which the preproAFP cDNA was inserted between the cauliflower mosaic virus 19S RNA promoter and the nopaline synthetase polyadenylation site. Although transgenic plants produced AFP mRNA, no AFP was detected on western blots. Re-evaluation of AFP expression in these transgenic plants showed that AFP accumulated to detectable levels only after exposure of the plant to cold. Extracts of plants incubated at 4°C for 24 h contained a protein which co-migrated with winter flounder proAFP and was cross-reactive to Type I AFP antisera. Two other minor protein bands of slightly higher apparent M r also cross-reacted with the antisera and are thought to represent processing intermediates. The proAFP was unique to the transgenic plants and was absent in extracts taken prior to cold exposure. AFP levels increased over the first 48 h of cold incubation then remained stable. Since the α-helix content of Type I AFP has been shown to decrease markedly at warmer temperatures, we postulate that Type I AFP stability in transgenic plants is dependent on its secondary structure.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00029012

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6

Electronic Resource

Heat shock induced proteins in plant cells (1979)

Barnett, Thomas ; Altschuler, Mitchell ; McDaniel, Carl N. ; [et al.]

Chichester [u.a.] : Wiley-Blackwell

Developmental Genetics 1 (1979), S. 331-340

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ISSN: 0192-253X

Keywords: heat-shock ; proteins ; tobacco ; soybean ; Life and Medical Sciences ; Genetics

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: Tobacco (Nicotiana tabacum) and soybean (Glycine max) tissue culture cells were exposed to a heat shock and protein synthesis studied by SDS-polyacrylamide gel electrophoresis after labeling with radioactive amino acids. A new pattern of protein synthesis is observed in heat-shocked cells compared to that in control cells. About 12 protein bands, some newly appearing, others synthesized in greatly increased quantities in heat-shock cells, are seen. Several of the heat-shock proteins (HSPs) in both tobacco and soybean are similar in size. One of the HSPs in soybean (76K) shares peptide homology with its presumptive 25°C counterpart, indicating that the synthesis of at least some HSPs may not be due to activation of new genes. The optimum temperature for maximal induction of most HSPs is 39-40°C. Total protein synthesis decreases as heat-shock temperature is increased and is barely detectable at 45°C. The heat-shock response is maintained for a relatively short time in tobacco cells. After 3 hr at 39°C, a decrease is seen in the synthesis of the HSPs, and after 4 hr practically no HSPs are synthesized. After exposure to 39°C for 1 hr, followed by a return of tobacco cells to 26°C, recovery to the control pattern of synthesis requires greater than 6 hours. These results indicate that cells of flowering plants exhibit a heat-shock response similar to that observed in animal cells.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/dvg.1020010406

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