MANIPULASI GEN PDII DENGAN CARA DELESI INTERNAL DAN PENGARUHNYA TERHADAP VIABILITAS SEL SACCHAROMYCES CEREVISIA
<b>Abstract:<p align=\"justify\"> <br /> <br /> Most secreted, cell surface and extracellular protein contain disulphide bonds. The function of disulphide bonds is to assist the folding, and to stabilize the tertiary and quaternary structure of protein. These bon...
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| Format: | Theses |
| Language: | Indonesia |
| Online Access: | https://digilib.itb.ac.id/gdl/view/4705 |
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| Institution: | Institut Teknologi Bandung |
| Language: | Indonesia |
| Summary: | <b>Abstract:<p align=\"justify\"> <br />
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Most secreted, cell surface and extracellular protein contain disulphide bonds. The function of disulphide bonds is to assist the folding, and to stabilize the tertiary and quaternary structure of protein. These bonds are formed in the endoplasmic reticulum lumen by dithiol oxidation and catalyzed by protein disulphide isomerase (PDI: EC 5.3.4.1). PDI also catalyzed reduction and isomerization of many protein substrates. PDI contains six specific areas (sites, domains), i.e.; signal peptide (ss), first active site (a), second active site (a\'), first putative binding site (b), second putative binding site (b\') and lumen endoplasmic reticulum retention site (c). In Saccharomyces cerevisiae PDI is encoded by PDII gene. PDII is an essential gene since disruption of the gene is haplo-lethal. The aim of the project is to study structure-function of PDI. pdil mutant was constructed by deletion of the a, b and b\' sites using restriction endonucleases enzyme NcoI. The gin] (pdilzlNcol) mutant was unable to support yeast growth. This investigation suggests that the a, b and b\' areas could be required for stability structure of PDI.<b>Abstrak:<p align=\"justify\"> <br />
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