Molecular biology of plant strees response
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The cellular stress response is evolutionarily conserved in all living organisms, and a major role is attributed to the induced heat shock proteins (Hsps) and other molecules that confer stress protection. The molecular responses elicited by the cells dictate whether the organism adapts, survives, or, if injured beyond repair, undergoes death. Most of the time these responses are beneficial to the organisms, but sometimes cells like cancer cells mount defensive mechanisms that interfere with therapies. Our detailed understanding of stress responses has paved the way for the development of stress-tolerant crops in several instances (Grover et al 1999). Considering all these, studies on stress responses turned out to have broad biological applications in microorganisms, plants, animals, and humans in health and in disease.
HEAT SHOCK PROTEINS
F. Ritossa discovered the heat shock response (Hsr) in Drosophila salivary glands in 1962. In 1974–1975 H. Mitchell and A. Tissières demonstrated that heat shock induced the expression of a set of new proteins under these conditions that were called the Hsps, and the induction of this response was subsequently found to be universal. For plants, early work on heat shock–induced alterations in protein profiles appeared independently from the groups of J.P. Mascarenhas and Joe L. Key.
Although the meeting formally started on 10 October 2001, a special introductory course was organized on 9 October to give a general overview in Spanish and English on molecular biology of stress responses, mainly for the local students from Latin America. This special course emphasized the following themes:
As several agents other than heat can also induce Hsr, the Hsps are also called stress proteins. In general, there are several classes of Hsps categorized according to their apparent subunit molecular weights, including a small Hsp family with molecular masses ranging from 14 kDa to 29 kDa, Hsp40 family, Hsp60 family, Hsp70 family, Hsp90 family, and Hsp110 family. Hsps are now recognized as important to a range of physiological and cellular functions under both normal growth conditions and in response to stresses other than heat shock. Characterization of the individual Hsp has also led to the realization that most cells contain constitutively expressed homologs of the inducible Hsp that are essential to specific Hsp functions.
Starting in the mid-1980s, the concept of molecular chaperones evolved from the work of biochemists and cell biologists, and several Hsps were soon recognized as having such chaperoning functions
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HEAT SHOCK PROTEINS
F. Ritossa discovered the heat shock response (Hsr) in Drosophila salivary glands in 1962. In 1974–1975 H. Mitchell and A. Tissières demonstrated that heat shock induced the expression of a set of new proteins under these conditions that were called the Hsps, and the induction of this response was subsequently found to be universal. For plants, early work on heat shock–induced alterations in protein profiles appeared independently from the groups of J.P. Mascarenhas and Joe L. Key.
Although the meeting formally started on 10 October 2001, a special introductory course was organized on 9 October to give a general overview in Spanish and English on molecular biology of stress responses, mainly for the local students from Latin America. This special course emphasized the following themes:
As several agents other than heat can also induce Hsr, the Hsps are also called stress proteins. In general, there are several classes of Hsps categorized according to their apparent subunit molecular weights, including a small Hsp family with molecular masses ranging from 14 kDa to 29 kDa, Hsp40 family, Hsp60 family, Hsp70 family, Hsp90 family, and Hsp110 family. Hsps are now recognized as important to a range of physiological and cellular functions under both normal growth conditions and in response to stresses other than heat shock. Characterization of the individual Hsp has also led to the realization that most cells contain constitutively expressed homologs of the inducible Hsp that are essential to specific Hsp functions.
Starting in the mid-1980s, the concept of molecular chaperones evolved from the work of biochemists and cell biologists, and several Hsps were soon recognized as having such chaperoning functions
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Here's your answer mate
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Response✍
- it is the reaction of an organism to a stimuli
✰Hope it helps❢❢
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