Impact of high CO2 levels on heat shock proteins during postharvest storage of table grapes at low temperature. Functional in vitro characterization of VVIHSP18.1

Abstract Etiolated maize radicles (inbred Oh43) subjected to a brief heat shock synthesize a family of small heat shock proteins (≃18 kD) that is composed of at least 12 members. We previously described the cDNA-derived sequence of three maize shsp mRNAs (cMHSP18-1, cMHSP18-3, and cMHSP18-9). In this report, we demonstrate that the mRNA transcribed in vitro from one of these cDNAs (cMHSP 18-9) is responsible for the synthesis of three members of the shsp family, and we suggest that cMHSP18-3 may be responsible for the synthesis of three additional members and cMHSP18-1 for the synthesis of two other members of this family. The fact that these genes do not contain introns, coupled with the observations reported herein, suggest that maize may have established another method of using a single gene to produce a number of different proteins.

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WRKY transcription factors in the response of table grapes (cv. Autumn Royal) to high CO2 levels and low temperature

Postharvest Biology and Technology ◽

10.1016/j.postharvbio.2018.12.011 ◽

2019 ◽

Vol 150 ◽

pp. 42-51 ◽

Cited By ~ 4

Author(s):

Irene Romero ◽

Estibaliz Alegria-Carrasco ◽

Alfonso Gonzalez de Pradena ◽

Maria Vazquez-Hernandez ◽

M. Isabel Escribano ◽

...

Keyword(s):

Transcription Factors ◽

Low Temperature ◽

Wrky Transcription Factors ◽

High Co2 ◽

Table Grapes ◽

Co2 Levels

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Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteins.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54835-3 ◽

1991 ◽

Vol 266 (31) ◽

pp. 21165-21173 ◽

Cited By ~ 3

Author(s):

D.B. Schowalter ◽

W.P. Sullivan ◽

N.J. Maihle ◽

A.D. Dobson ◽

O.M. Conneely ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Progesterone Receptor ◽

Receptor Binding ◽

Shock Proteins

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Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60

Biochemical Journal ◽

10.1042/bj20050861 ◽

2005 ◽

Vol 391 (2) ◽

pp. 185-190 ◽

Cited By ~ 64

Author(s):

Renu Wadhwa ◽

Syuichi Takano ◽

Kamaljit Kaur ◽

Satoshi Aida ◽

Tomoko Yaguchi ◽

...

Keyword(s):

Heat Shock ◽

Molecular Interactions ◽

Heat Shock Protein 60 ◽

Hsp60 Expression ◽

Mitochondrial Hsp70 ◽

Shock Proteins ◽

First Time

Mortalin/mtHsp70 (mitochondrial Hsp70) and HSP60 (heat-shock protein 60) are heat-shock proteins that reside in multiple subcellular compartments, with mitochondria being the predominant one. In the present study, we demonstrate that the two proteins interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions. Suppression of HSP60 expression by shRNA (short hairpin RNA) plasmids caused the growth arrest of cancer cells similar to that obtained by suppression of mortalin expression by ribozymes. An overexpression of mortalin, but not of HSP60, extended the in vitro lifespan of normal fibroblasts (TIG-1). Taken together, this study for the first time delineates: (i) molecular interactions of HSP60 with mortalin; (ii) their co- and exclusive localizations in vivo; (iii) their involvement in tumorigenesis; and (iv) their functional distinction in pathways involved in senescence.

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A family of related proteins is encoded by the major Drosophila heat shock gene family

Molecular and Cellular Biology ◽

10.1128/mcb.2.3.286-292.1982 ◽

1982 ◽

Vol 2 (3) ◽

pp. 286-292

Author(s):

S C Wadsworth

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Protein ◽

Sodium Dodecyl ◽

Heat Shock Gene ◽

Partial Digestion ◽

Shock Gene ◽

Shock Proteins

At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.

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