Search for dissertations about: "RNase"
Showing result 1 - 5 of 69 swedish dissertations containing the word RNase.
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1. Post-transcriptional regulation by RNases in Streptococcus pyogenes
Abstract : Ribonucleases (RNases) are proteins that adjust cellular RNA levels by processing RNA transcripts, leading to their stabilization or degradation. RNases are grouped based on their ability to cleave the transcript internally (endoRNases) or degrade the transcript starting from the ends (exoRNases). READ MORE
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2. EF-Tu and RNase E : Essential and Functionally Connected Proteins
Abstract : The rate and accuracy of protein production is the main determinant of bacterial growth. Elongation Factor Tu (EF-Tu) provides the ribosome with aminoacylated tRNAs, and is central for its activity. In Salmonella enterica serovar Typhimurium, EF-Tu is encoded by the genes tufA and tufB. READ MORE
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3. Investigation of RNase P active site residues and catalytic domain interaction
Abstract : RNase P is an essential endoribonuclease responsible for the maturation of the tRNA 5’end. The RNase P family encompasses the ribozyme based, RNase P RNP, and proteinaceous RNase P (PRORP). The ribozyme based RNase P is widely distributed in most species while PRORP has so far mainly been found in some eukaryotic cells. READ MORE
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4. Metal ion cooperativity in Escherichia coli RNase P RNA
Abstract : RNase P is an essential ribonuclease responsible for removal of the 5’ leader of tRNA precursors. Bacterial RNase P consists of an RNA subunit and a small basic protein. The catalytic activity is associated with the RNA subunit, i.e. READ MORE
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5. Distal to Proximal—Functional Coupling in RNase P RNA-mediated Catalysis
Abstract : RNase P is a ubiquitous ribonuclease responsible for removing the 5’ leader of tRNA precursor. Bacterial RNase P contains one RNA (RPR) and one protein (RPP) subunit. However, the number of protein variants depends on the origin. The RNA subunit is the catalytic subunit that in vitro cleaves its substrate with and without the protein subunit. READ MORE