Open Access. Powered by Scholars. Published by Universities.®

Molecular Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

Articles 1 - 2 of 2

Full-Text Articles in Molecular Biology

Characterization Of Splicing Mechanisms By Single-Molecule Fluorescence, Krishanthi Sanjeewani Karunatilaka Jan 2011

Characterization Of Splicing Mechanisms By Single-Molecule Fluorescence, Krishanthi Sanjeewani Karunatilaka

Wayne State University Dissertations

Group II introns rank amongst the largest self-splicing ribozymes found in bacteria and organellar genomes of various eukaryotes. Despite the diversity in primary sequences, group II introns posses highly conserved secondary structures consisting of six domains (D1-D6). To perform its function, the large multidomain group II intron RNA must adopt the correctly folded structure. As a result, in vitro splicing of these introns requires high ionic strength and elevated temperatures. In vivo, this process is mainly assisted by protein cofactors. However, the exact mechanism of protein-mediated splicing of group II intron RNA is still not known.

In order to elucidate ...


Investigating The Metal Binding Sites In Znta, A Zinc Transporting Atpase, Sandhya Muralidharan Jan 2010

Investigating The Metal Binding Sites In Znta, A Zinc Transporting Atpase, Sandhya Muralidharan

Wayne State University Dissertations

ZntA from Escherichia coli is a member of the PIBtype ATPase family of transporters. The PIB-type ATPase pumps maintain cellular homeostasis of heavy metals such as Zn2+, Co2+, Cu2+, Cu+, and mediate resistance to toxic metals such as Pb2+, Cd2+ and Ag+. ZntA confers resistance to Pb2+, Cd2+, and Zn2+ by pumping these ions out of the cytoplasm. ZntA has two metal binding sites, one in the hydrophilic N-terminal domain and the other in the transmembrane region. The cysteine-rich N-terminal domain has ~110 amino acids and the conserved ...