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The Heterologous Expression Of Lily SHsp16.45and Its Functional Analysis

Posted on:2013-03-08Degree:MasterType:Thesis
Country:ChinaCandidate:S J ZhangFull Text:PDF
GTID:2230330371986797Subject:Cell biology
Abstract/Summary:PDF Full Text Request
Suffering from the high temperature, low temperature or drought stress, the plant can produce heat shock protein (Hsp). The protein whose molecular weight is among12~42kD is called small heat shock protein (sHsp). Almost all kind of Hsp always has a conservative ACD domain on the structure. Heat shock protein, one kind of molecular chaperones in adversity stress, can protect the functional proteins from irreversible degeneration, maintain the folding structure of natural protein and promote the proteins that have already folded in wrong way or depolymerized from the right protein conformation to recovery or degradation. The role of small heat shock protein in plant has become one of the most important research directions in recent years.Our research made use of Lily small heat shock protein-LimHsp16.45for heterologous expression. We found that LimHsp16.45can improve the cell activity of E.coli effectively under high or low temperature stress. And we also observed the accumulation of this sHsp increased after heat treatment. In Arabidopsis, LimHsp16.45is located on inner membrane system. It can not only respond the heat stimulus and form typical heat shock Granules (HSGs), but also improve seed germination ratio in high-salt-stress. LimHsp16.45can increase the tolerance against oxidative stress. We observed that HSGs also exist when seedlings of Arabidopsis grow in high-salt-stress. So we speculate that LimHsp16.45in salt stress response also play the physiological function by forming oligomers.
Keywords/Search Tags:sHsp, chaperone, heterologous expression, oligomers, HSGs
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