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Up Regulation of Heat Shock Protein 70B (HSP70B) and <em>SSA1</em> in <em>Chlamydomonas Reinhardtii</em> via HSP70A-RBCS2 and PSAD PromoterAmos, B. Kirtley 01 January 2015 (has links)
Fabrication of effective algae cultivation systems adjacent to coal-fired power plants to fixate waste CO2 would represent a sizable step towards achieving a carbon neutral energy cycle. However, emission gas would elevate the algal cultivation system temperature and decreases its pH without expensive preprocessing. Increased temperature and acidity constitutes a profound stress on the algae. Although stressed algae produce heat shock proteins (HSPs) that promote protein folding and protect against stress, the ordinary biological response is insufficient to protect against coal flue gas. Experimental upregulation of HSPs could make algae respond to the stress caused by high temperatures and low pH at an elevated level. However, no work has been done to determine whether HSPs can be experimentally upregulated in algae. Here, the Chlamydomonas reinhardtii algal strain was selected because it has a sequenced genome and singular cell structure ideal for genetic modifications. Two genetic modification methods: transformation with plasmids pCB720/pCB740, and cloned pchlamiRNA3/pchlamiRNA3int with yeast HSP gene SSA1 were evaluated. pCB720/pCB740 up regulate algae production of native HSP, HSP70B. pCB720 transformation success was observed but statistically, data varied. pchlamiRNA3/pchlamiRNA3int were cloned with SSA1. Chlorophyll content measured growth indirectly. Quantitative HSP detection could be done using RT-PCR.
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