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Determinants of Structural Organization and Substrate Specificity in Ribonuclease P
Başlık:
Determinants of Structural Organization and Substrate Specificity in Ribonuclease P
Yazar:
Chan, Clarence W., author.
ISBN:
9780438115941
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (676 pages)
Genel Not:
Source: Dissertation Abstracts International, Volume: 79-11(E), Section: B.
Advisors: Alfonso Mondragon Committee members: John Marko; Ishwar Radhakrishnan; Amy Rosenzweig.
Özet:
Determinants of Structural Organization and Substrate Specificity in Ribonuclease P Clarence W. Chan Ribonuclease Precursor (ribonuclease P or RNase P) is an endonucleolytic ribonucleic acid enzyme (ribozyme) that is conserved across all domains of life. The primary and most well-studied function of RNase P is its role in transfer RNA (tRNA) biogenesis, as it catalyzes the removal of an extraneous 5' leader segment from precursor tRNAs. Previous studies have also shown that RNase P, which consists of a catalytic RNA subunit and at least one protein cofactor, can act on a variety of RNA substrates in addition to precursor tRNAs. The precise mechanism by which RNase P recognizes and distinguishes tRNAs and other non-tRNA substrates from the diverse pool of folded RNA molecules in a typical cell remains unclear, particularly when considering that some of its non-tRNA substrates are predicted to assume a completely different tertiary structure than tRNAs.
My approach to studying the substrate specificity of RNase P was to examine structurally how bacterial RNase P recognizes alternative non-tRNA substrates, as well as to investigate the structure and function of additional protein subunits that are unique to the archaeal and eukaryotic RNase P to better define the intricate relationships among substrate specificity, catalytic function, and structural organization of the RNase P macromolecular complex in the three domains of life. My work on RNase P and its various RNA substrates has provided me with a unique perspective to analyze several RNA motifs, such as tetraloops, T-loops, and K-turns, as well as recurrent patterns of structural organization in large RNA and RNA-protein complexes.
Taken together, my studies provide not only novel insights into the determinants of structural organization and substrate specificity in RNase P, but also a better understanding of the biophysical properties of folded RNAs and their interactions with proteins. Although my work spans a multitude of systems and involves a large collection of biological molecules, I present my work with the unified theme that folded RNA molecules are structurally and functionally diverse, assume critical roles for a wide range of cellular processes, and have co-evolved with a large supporting cast of fascinating protein cofactors and modifying enzymes. Thesis advisor: Dr. Alfonso Mondragon.
Notlar:
School code: 0163
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(688947.1) | 688947-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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