THE ROLE OF ELONGATION FACTORS IN GENE TRANSLATION AND PROTEIN SYNTHESIS. Professor Kinzy’s lab seeks to investigate the structure and function of G- protein in relation to it’s regulation and the post transcriptional processes associated with gene expression. The lab uses Translation Elongation apparatus found in yeast to investigate these processes. The components of these elongation factors are important targets for antibacterial and antifungal drugs such that improper expressions and mutations in these factors can cause several forms of Carcinoma; a type of cancer that develops from epithelial cells or tissues that line the outer surface of the body. Mutations could also affect protein synthesis and viral replication.
The team track the …show more content…
The lab focuses on three types of eEFs; eEF1, eEF2 and eEF3 with most focus on the eEF1 which is the prototype of G- proteins. The EF1Alpha (eEF1A), a component of EF1 is GTP- dependent and its function is to accurately attach aminoacyl-tRNA to the ribosome. The other component of eEF1 is the eEF1Balpha, a guanine nucleotide exchange factor (GEF) found in yeast. Its function is to catalyze the exchange of GDP for GTP to maintain the pool of active protein. The use eEF1B free genetic system allows Professor Kinzy’s labs to manipulate eEF1 without the GEF in order to understand how G- proteins are regulated. The introduction of of eEF1B mutants into the genetic system allow the lab to analyze the processes associated with guanine nucleotide exchange and the effects of changes in protein activity. The last component is eEF1Bgamma which plays a role in the sensitivity of the cell to oxidative stress and …show more content…
During the elongation stage, the peptide chain increases its length by cyclically adding one amino acid at a time. This process is controlled by eEF1 which catalyzes the delivery of aa- tRNA (1) to the site of elongation. eEF2 allows the ribosome to move down the mRNA one codon at a time by acting a translocase (1). Aside these functions, components of the eEF1 have been found to play other roles in the cell. eEF1A has been identified as an actin binding protein. Competitive binding experiments with eEF1A, F-actin and aa-tRNA showed that as pH increases, the affinity of eEF1A for F-actin decreased while that for aa-tRNA increased (2). A previous work done by the Kinzy lab two classes of eEF1A mutants were generated. Class one mutants, N305S- and N329S-Ura3p, were found to maintain normal levels of global translation while exhibiting disorganization of actin cytoskeleton. Class two mutants, F308L- and S405P-Ura3p exhibited defects in translation and cytoskeleton. (3) eEF1Bgamma has been show to have no significant effect on translation when it is removed from the cell. It is, however, a suppressor of cold- sensitive mutations of DRS2 which plays a role in Golgi budding (4). Strains free from the eEF2Bgamma were found to show protein expression that differed when compared to their wild types under stressful
The team track the …show more content…
The lab focuses on three types of eEFs; eEF1, eEF2 and eEF3 with most focus on the eEF1 which is the prototype of G- proteins. The EF1Alpha (eEF1A), a component of EF1 is GTP- dependent and its function is to accurately attach aminoacyl-tRNA to the ribosome. The other component of eEF1 is the eEF1Balpha, a guanine nucleotide exchange factor (GEF) found in yeast. Its function is to catalyze the exchange of GDP for GTP to maintain the pool of active protein. The use eEF1B free genetic system allows Professor Kinzy’s labs to manipulate eEF1 without the GEF in order to understand how G- proteins are regulated. The introduction of of eEF1B mutants into the genetic system allow the lab to analyze the processes associated with guanine nucleotide exchange and the effects of changes in protein activity. The last component is eEF1Bgamma which plays a role in the sensitivity of the cell to oxidative stress and …show more content…
During the elongation stage, the peptide chain increases its length by cyclically adding one amino acid at a time. This process is controlled by eEF1 which catalyzes the delivery of aa- tRNA (1) to the site of elongation. eEF2 allows the ribosome to move down the mRNA one codon at a time by acting a translocase (1). Aside these functions, components of the eEF1 have been found to play other roles in the cell. eEF1A has been identified as an actin binding protein. Competitive binding experiments with eEF1A, F-actin and aa-tRNA showed that as pH increases, the affinity of eEF1A for F-actin decreased while that for aa-tRNA increased (2). A previous work done by the Kinzy lab two classes of eEF1A mutants were generated. Class one mutants, N305S- and N329S-Ura3p, were found to maintain normal levels of global translation while exhibiting disorganization of actin cytoskeleton. Class two mutants, F308L- and S405P-Ura3p exhibited defects in translation and cytoskeleton. (3) eEF1Bgamma has been show to have no significant effect on translation when it is removed from the cell. It is, however, a suppressor of cold- sensitive mutations of DRS2 which plays a role in Golgi budding (4). Strains free from the eEF2Bgamma were found to show protein expression that differed when compared to their wild types under stressful