Characterization of the Methanococcus jannaschii RNase P holoenzyme.
| dc.contributor.advisor | J.W. Brown, Chair | en_US |
| dc.contributor.advisor | L. Parks, Member | en_US |
| dc.contributor.advisor | P. Wollenzien, Member | en_US |
| dc.contributor.author | Andrews, Andrew J. | en_US |
| dc.date.accessioned | 2010-04-02T18:04:57Z | |
| dc.date.available | 2010-04-02T18:04:57Z | |
| dc.date.issued | 2000-08-10 | en_US |
| dc.degree.discipline | Microbiology | en_US |
| dc.degree.level | Master's Thesis | en_US |
| dc.degree.name | MS | en_US |
| dc.description.abstract | The RNase P RNAs from Methanococcus and Archaeoglobus lack secondary structural features essential for the recognition of pre-tRNA. In the absence of protein, these RNase P RNAs lack catalytic activity. How the Methanococcus and Archaeoglobus RNase P holoenzymes compensate for the absent RNA structural elements is not known, but we hypothesize that it is via additional proteins. The Methanococcus jannaschii RNase P holoenzyme has been purified for structural and functional characterization. This enzyme has a buoyant density in Cs2SO4 of 1.39 g/ml and an apparent molecular weight of greater than 400kDa. The holoenzyme has a Km of 68 nM, a kcat of 37nM min-1 (similar to that of other RNase P enzymes) and tolerates a wide range of ionic conditions. Six potential protein subunits have been identified on the basis of copurification with enzymatic activity. The molecular weight of three of these bands is consistent with apparent holomologs of RNase P proteins from Methanobacterium thermoautotrophicum and Saccharomyces cerevisiae. | en_US |
| dc.identifier.other | etd-20000810-110103 | en_US |
| dc.identifier.uri | http://www.lib.ncsu.edu/resolver/1840.16/1540 | |
| dc.rights | I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. | en_US |
| dc.title | Characterization of the Methanococcus jannaschii RNase P holoenzyme. | en_US |
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