2026-09-21T18:11:39Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/93021 2023-07-11 col_2142_14789 col_2142_5131 com_2142_14788 com_2142_8903 com_2142_5130

Gennis, Robert B. Imlay, James A. Oldfield, Eric Oldfield, Eric Jin, Hong Rao, Guodong 2016-11-10T18:39:14Z 2016-11-10T18:39:14Z 2018-11-11T10:15:32Z 2016-06-28 2016-08 "The protein IspH, (E)-1-hydroxy-2-methyl-but-2-enyl 4-diphosphate reductase, is an essential enzyme in isoprenoid biosynthesis and an important drug/herbicide target. The main research in this work investigated the structures and functions of IspHs from various organisms. Using a sequence similarity network we found that some IspHs form ""Rosetta-stone"" fusion proteins with either the ribosomal protein S1 (RPS1), or a UbiA (4-hydroxybenzoate octaprenyltransferase)-like protein. These fusion proteins are all from obligately anaerobic bacteria. A catalytically active IspH-RPS1 was expressed and characterized. The existance of these fusion proteins is indicative of possible secondary roles of the enzyme IspH, perhaps being involved in O2 sensing and regulation. Using crystallographic and bioinformatics results we show that IspHs can be classified into four major classes, based on the arrangement of the aromatic residues near the 4Fe-4S cluster and the presence of N- and C-terminal extensions, and these structure features are related to the environments in which IspHs are found. These aromatic groups protect the 4Fe-4S clusters from oxidation and are also involved in electron transfer. The results revealed how nature has evolved different structure features for a sensitive protein in different environments. In addition, another terpene biosyntheis enzyme, MenA, and two other metalloenzymes that are drug targets, DHAD and LOX, were also investigated. Overall, this research is of interest since it revealed the structure and functions of the terpene biosynthesis enzyme IspH from various organisms, as well as other proteins that are possible drug targets." Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2018-08-01 The student, Guodong Rao, accepted the attached license on 2016-06-27 at 21:31. The student, Guodong Rao, submitted this Dissertation for approval on 2016-06-27 at 21:37. This Dissertation was approved for publication on 2016-06-28 at 15:33. DSpace SAF Submission Ingestion Package generated from Vireo submission #9715 on 2016-11-10 at 12:24:45 Made available in DSpace on 2016-11-10T18:39:14Z (GMT). No. of bitstreams: 3 RAO-DISSERTATION-2016.pdf: 7364430 bytes, checksum: eae4f216380cf82aeade34af0d8dffe1 (MD5) LICENSE.txt: 4208 bytes, checksum: cd02dd892dabb20b90058d99d1252ebd (MD5) PROQUEST_LICENSE.txt: 4554 bytes, checksum: f893ea1904563a50d2f70a2a866c45fa (MD5) Previous issue date: 2016-06-28 Embargo set by: Seth Robbins for item 95443 Lift date: 2018-11-10T18:39:22Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system Embargo set by: Seth Robbins for item 95443 Lift date: 2018-11-10T18:43:22Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system U of I Only Restriction Lifted for Item 95443 on 2018-11-11T10:15:32Z. application/pdf http://hdl.handle.net/2142/93021 en Copyright 2016 Guodong Rao IspH Iron-sulfur cluster Infectious diseases Metalloenzymes Structure and function of the terpene biosynthesis enzyme, IspH text text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.