2026-09-20T03:45:16Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/86740 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Daniel W. Celander True-Krob, Heather Leigh 2015-09-28T15:17:45Z 2015-09-28T15:17:45Z 10000-01-01 1998 1998 Photochemical crosslinking experiments with a photoaffinity-labeled substrate have been performed with the RNase P RNA subunit and holoenzymes from various sources. Experimental studies clearly reveal that the prokaryotic RNA subunit is involved in substrate binding, but that the eukaryotic RNA subunit alone is unable to bind substrate. Crosslinking experiments with the holoenzyme from various sources suggest that protein components of the eukaryotic holoenzyme contribute to the active site architecture and may mediate substrate binding functions. Thus, one role of the protein subunit in the eukaryotic RNase P may be simply to recognize and bind precursor tRNAs and position them into the holoenzyme active site for correct cleavage. To further understand the differences in substrate-binding capability of RNase P RNA subunits from various sources, chimeric molecules were constructed and analyzed. These molecules are comprised of the human (HeLa) subunit backbone with small structural regions replaced with structures from the catalytic Bacillus subtilis RNA. This data suggests that the inability to generate a specific region of tertiary structure in the RNA may be important in the ability to form a structure competent for binding RNA substrates. Made available in DSpace on 2015-09-28T15:17:45Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9912401.pdf: 5583516 bytes, checksum: bc37e8da9278e892c9eb9d315467607d (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 88021 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 153 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/86740 (MiAaPQ)AAI9912401 eng Chemistry, Biochemistry Biochemical Studies of Ribonuclease P of Tetrahymena Thermophila text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.